Albert Neuberger. 15 April 1908 −− 14 August 1996: Elected ...rsbm.royalsocietypublishing.org/content/roybiogmem/47/369.full.pdf · Albert Neuberger. 15 April 1908 −− 14 ...

F.R.S. 1951 14 August 1996: Elected−−Albert Neuberger. 15 April 1908

Anthony K. Allen and Helen M. Muir

, 369-382, published 1 November 2001472001 Biogr. Mems Fell. R. Soc.

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ALBERT NEUBERGER

15 April 1908 — 14 August 1996

Biog. Mems Fell. R. Soc. Lond. 47, 369–382 (2001)

on May 14, 2018http://rsbm.royalsocietypublishing.org/Downloaded from




ALBERT NEUBERGER

15 April 1908 — 14 August 1996

Elected F.R.S. 1951

B A K. A1 HM. M

2, C.B.E., F.R.S.

1Molecular Pathology Section, Division of Biomedical Sciences,

Imperial College School of Medicine, Sir Alexander Fleming Building,

South Kensington, London SW7 2AZ, UK2Langlands House, Hornby, Bedale, North Yorkshire DL8 1NG, UK

B

Albert Neuberger was born in 1908 in the small Franconian town of Hassfurt, which is in thenorth of Bavaria. At the time of Albert’s birth, the Kingdom of Bavaria was a semi-autonomous state of the German Empire.

His parents were Max Neuberger and Bertha, née Hiller. His ancestors on both sides hadbeen in the region for several generations and were small-town business people with aninterest in scholarship and local affairs. They were religious Jews with a strict, somewhatVictorian, sense of moral values, who mixed freely and without any self-consciousness withtheir Christian neighbours.

He had a happy, secure childhood and was very close to both his parents. He described hisfather as being a businessman who was more interested in a variety of intellectual activitiesthan in his business. Albert was the eldest of three children. He attended the local elementaryschool from the age of six, but had already been writing German and Hebrew from the age offive. At the age of nine he was sent to a secondary school in Würzburg. However, the end ofWorld War I brought about difficult conditions in the larger towns and he was therefore takenback to Hassfurt, which was peaceful and had a good supply of food. For the next four or fiveyears he was taught by a variety of tutors including the local Protestant pastor. He received agood grounding in Latin, Greek, Hebrew, mathematics and history, but no science. By the endof 1923 he was able to return to Würzburg to attend the Neue Gymnasium (high school). (Ona visit to Würzburg in the 1990s he was shown his name on the board of honour in his old

371 © 2001 The Royal Society



372 Biographical Memoirs

school.) For the most part he studied classics but also had good teaching in mathematics andphysics. He was not taught any chemistry or biology. He said in later life that he neverregretted the time spent on Latin and Greek and that he regarded classical studies as being anexcellent background for any academic study.

At the age of 18 he entered the University of Würzburg as a law student, with theintention of later following an academic career and concentrating on the history andphilosophy of law. However, during his first term he began to doubt the wisdom of his choice,started to attend science lectures and became particularly interested in physiology. In thesecond term he transferred to the preclinical medicine course, took enthusiastically tochemistry and biochemistry, and passed with distinction in 1928. He made his clinical studiesin Würzburg and Berlin, passed all his examinations with distinction and was awarded anM.D. summa cum laude, in 1931. This MD work also resulted in the publication of his firsttwo scientific papers on intracellular proteolysis (1, 2)*.

During his time as a student in Berlin he devoted much of his spare time and his longvacations to working in the laboratory of Professor Peter Rona, who introduced him to themodern aspects of biochemistry. His periods in Berlin (1928–32) were a crucial time inGerman history. Having come from a conservative south German city he was rather shockedby the liberated social and sexual culture, but he also found the atmosphere culturallystimulating. He felt that the pre-1914 values had disappeared but had not been replaced in asatisfactory manner. This was particularly noticeable in politics, in which a situation arose oftwo violent extreme parties, the Nazis and the Communists, who were squeezing out themoderate political groups. He therefore feared that Germany was heading towards either aleft-wing or right-wing totalitarian regime and he felt that it would be impossible to live undereither.

After completion of his medical examinations, from 1931 to 1932, he did 18 months ofclinical work in Frankfurt and Würzburg in the equivalent position to a house officer.Although he enjoyed clinical work, he decided to return to Rona’s laboratory in October 1932for further laboratory experience. However, there was then a rapid deterioration in thepolitical situation, so with Rona’s introductions he visited laboratories in Amsterdam andLondon. He became convinced that he would be happy to live in England but returned toBerlin without having made a final decision. In Berlin it then became obvious to him that theNazis were going to gain power and at the end of 1932 he moved permanently to London.This was a wise decision, as on 30 January 1933 Adolf Hitler became Chancellor of Germany.

In the next six years his immediate family managed, with his help, to leave Germany. Hissister, who was five years younger, had followed him to medical school in Würzburg but wasexpelled by the Nazis in 1934, before completion of her studies. She migrated to Palestine andbecame a farmer’s wife. His brother, who was 10 years younger, moved via England to theUSA and became a well-known rabbi. His father had died in 1931; his mother andgrandmother survived rather precariously in Würzburg until 1938, when he was able to bringthem to England.

He was obviously not forgotten by the German authorities because his name appeared ona rather distinguished list of 2820 residents of the UK that was compiled by the Gestapo in1940. These were people who were to be arrested as soon as possible after the Germaninvasion, which was scheduled for the autumn of that year.

* Numbers in this form refer to the bibliography at the end of the text.



Albert Neuberger 373

C

With an introduction from Professor Rona he was able to start work in the laboratory ofProfessor C.R. (later Sir Charles) Harington, F.R.S., at University College Hospital, London.His work on the electrochemistry of amino acids and proteins was also greatly influenced bythe distinguished physical chemist Professor F.G. Donnan, F.R.S., who was at UniversityCollege London. Neuberger was supported by a grant from the Academic Assistance Council,which had been founded in 1933 and was financed by a remarkable collective act of generosityof university staff to help academic refugees from Europe. He gained a PhD in 1936 and wasthen awarded a Beit Memorial Research Fellowship so that he could continue to work atUniversity College Hospital Medical School. He remained there until 1939, working on thequestion of whether sugars were true components of ‘normal’ proteins.

At the outbreak of war he was invited by Sir Frederick Gowland Hopkins, F.R.S., to jointhe Biochemistry Department at Cambridge. As this was one of the world centres forbiomedical research he found this to be a very stimulating environment, not only for thebiochemical discussions but also in the opportunities to meet historians, linguists andphilosophers. He also enjoyed involvement in the teaching of biochemistry for Part II of theCambridge Tripos.

As he had been told that he could not join the armed forces because he was in a reservedoccupation, he felt under an obligation to do some work that was of direct value to the nationin time of war. After some initial research on adhesives for the Royal Air Force, he decided,after discussions with Sir Charles Martin, Director of the Lister Institute, to work on thenutritional value of the potato. He was joined in this work by a newly graduated studentcalled Fred Sanger (subsequently a double Nobel laureate; F.R.S. 1954), who became his firstPhD student. Apart from the work on potato, they both had an interest in the fundamentalsof protein structure. Neuberger had an interest in insulin and they derivatized it with benzenesulphonyl chloride to confirm previous indications that phenylalanine was an amino-terminalend-group of insulin. Sanger later independently developed the use of fluorodinitrobenzeneas an end-group reagent for sequencing studies. Sanger (1988) said of him:

I regard Albert as my main teacher. The most important thing he taught me, both by instruction andexample, was how to do research. I shall always be grateful for his kindness and patience. He also hadan extremely wide knowledge of biochemistry, which I admired and used but could never emulate.

In January 1943, at the invitation of Harington, he joined the Medical Research Council’sNational Institute for Medical Research (NIMR) (initially at Hampstead and later at MillHill), where he was in charge of the Biochemistry Division until 1954. His initial research wason protein nutrition and the requirements for amino acids in conditions of starvation, injuryand burns. Later work was on amino-acid and porphyrin synthesis (see below).

Early in 1945 he went to India as consultant in nutrition to the Indian Army. To give himsufficient status with the military establishment he was appointed to the rank of Brigadier. Ashe remarked, rarely had promotion been so rapid, as his previous rank had been that ofLance Corporal in the Home Guard. He was there for four months, during which time hetravelled very extensively and advised on many nutritional problems. He also pointed out thatpopulation growth was likely to be a major problem for the future, a viewpoint that was notgenerally recognized then. In fact, at that time, the medical establishment in India wasconcerned about a predicted decrease in population.




In 1954 he was invited to fill the newly created Chair of Chemical Pathology at St Mary’sHospital Medical School, London, where he remained for 18 years. He had decided, with hisqualifications in both science and medicine, that he wished to return to a more clinicalenvironment and he was offered a position where the teaching and administrative burdenswere not too heavy. He was in overall charge of routine chemical pathology, but was able todelegate the day-to-day responsibilities to others. He enjoyed being in touch with the clinicalenvironment but was very happy to be able to build up research groups working onporphyrins, glycoproteins and carbohydrates.

During his time at St Mary’s he also accepted the request to become Principal of theWright–Fleming Institute at St Mary’s. In this post he upset some of the staff by hisassessments of their work, because they were not used to being subjected to critical appraisal.He also recruited new staff of very high quality, one of whom was Rodney Porter (F.R.S.1964), the future Nobel prizewinner. Porter was recruited from NIMR, Mill Hill, to the newChair of Immunology in 1959 despite the objections of some members of the selectioncommittee that a candidate without medical qualifications should not be appointed to a chairin the Wright–Fleming Institute (see Perry 1987).

On retirement he continued his research in the Biochemistry Department of the CharingCross Hospital Medical School. During these periods he held many other important postsincluding the chairmanship of the Lister Institute. In addition, he had close associations withthe Weizmann Institute and Hebrew University of Jerusalem.

R

Throughout his life, Albert Neuberger showed an unusually broad interest in science andmedicine. He made highly significant contributions in the areas of the chemistry andbiochemistry of amino acids (especially of glycine, serine, tryptophan and hydroxyproline),nutrition (with particular regard to amino acids and proteins), porphyrin biosynthesis, thechemistry of sugars (particularly amino sugars), lysozymes, lectins and especiallyglycoproteins (see (55) for summary).

Glycoproteins and lectins

His pioneering work on glycoproteins started in 1936 (4). At that time most biochemists feltthat, with the possible exception of mucins, the carbohydrate that could be detected in proteinpreparations was just an impurity. Neuberger felt that because many proteins gave a positivereaction in the Molisch reaction, which is specific for carbohydrate, at least some of theseproteins were likely to have covalently attached sugars He chose to investigate hen egg-whitealbumin because it was readily available and could be crystallized. Before chromatographyhad been developed, the only possible purification method was by repeated (sevenfold)crystallization until the preparation had a constant ratio of protein to carbohydrate. He thensubjected the ovalbumin to exhaustive proteolytic digestion followed by acetylation andsolvent extraction to remove the free amino acids from the digest. He was able to isolate acompound with a molecular mass of ca. 1200 Da. He determined its composition and foundthat it contained four molecules of mannose and two of N-acetylglucosamine. Its nitrogencontent indicated that there was another component present with two nitrogen atoms. Theseexperiments established that carbohydrate was attached covalently to ovalbumin and that itwas present mainly as a hexasaccharide. The linking amino acid was suspected by Neuberger




to be asparagine or glutamine, but with the techniques available at that time and also with theoutbreak of war he was not able to pursue the investigation.

This problem was taken up again in the 1950s with R.D. Marshall and P.G. Johansen(25, 26), and they were able to prove with other co-workers that the linkage between theprotein and carbohydrate moieties was between the amide of asparagine and the reducingcarbon atom of N-acetylglucosamine (27, 32–36, 39). His group then synthesized the linkagecompound, which established the structure beyond any doubt (28). This has subsequentlybeen shown to be a conserved linkage structure in all animals, plants and protozoa.

In 1965–66, together with Robin Derek Marshall, an attempt was made to establish theparticular amino-acid sequences in proteins that could lead to glycosylation. They showedthat the sequence Asn–Xaa–Ser (or Asn–Xaa–Thr), where Xaa can be any amino acid exceptproline or cysteine, was required for the N-glycosylation of asparagine with N-acetylglucosamine (43).

His work on lectins was initiated by Nathan Sharon, who spent six months in Neuberger’slaboratory in 1971, and followed on from work in the laboratory on the carbohydrate-bindinglysozymes. The work was in collaboration with Tony Allen and started on wheatgermagglutinin. It was concluded that the lectin was a cysteine-rich protein with an extendedbinding site with subsites for oligosaccharides of N-acetylglucosamine resembling thelysozymes. This was the first of the chitin-binding lectins to be purified (44).

Other lectins with similar specificities from potato and related plants were shown tocontain not only a cysteine-rich domain similar to wheatgerm agglutinin but also a highlyglycosylated hydroxyproline-rich region and has a collagen-like polyproline II structure that isstabilized by glycosylation (45, 47–54).

Other studies were made on extensively characterizing lectins from Vicia faba, pea andlentil. It was concluded that they differed from concanavalin A in that they strongly bound 3-O-methylhexoses, indicating that there is a strong hydrophobic interaction in the binding site(46). These observations led to structural studies by X-ray crystallography, which confirmedthe general conclusions.

A urinary glycoprotein was described by Tamm & Horsfall (1950). Neuberger’s groupcharacterized the glycoprotein and showed that it contained ca. 30% carbohydrate, was veryrich in sialic acids and was produced by kidney cells in culture (40–42).

Amino sugars

In his work on glycoproteins he became interested in the chemistry of sugars, particularly ofglucosamine and its derivatives. He prepared the methylglycosides of glucosamine and N-acetylglucosamine. The only previous work on this compound had been done by Irvine andco-workers (Irvine et al. 1911; Irvine & Hynd 1912), who had prepared the compound andhad concluded that methylglucosamine did not have a normal glycosidic structure because ofits unusually strong resistance to acid hydrolysis. In 1938, with Moggridge, Neubergerproposed that the compound did have a normal glycosidic linkage and that the resistance toacid hydrolysis in comparison with neutral sugars was due to an electrostatic effect from apositively charged amino group. In kinetic experiments they showed that the rate of hydroysisof methylglucosaminide was ca. 1% of that of the uncharged methyl glucoside. In a laterpaper in 1940 (5) he proved by O-methylation analysis that glucosamine really was 2-amino-2-deoxyglucose and that its glycosides were pyranosides. This work was fundamental to manysubsequent studies on the structure of glycoproteins.




Studies on the ionization of sugars were continued in his laboratory in the 1970s, not onlyof the amino group, but also of the acetamido and hydroxyl groups. Separations of sugarderivatives on ion-exchange columns were explained in terms of differential ionizations ofhydroxy groups.

Electrochemistry of amino acids and proteins

His PhD work was concerned with the dissociation constants of amino acids, particularlyglutamic acid and its esters, and he retained an active interest in this field throughout hiscareer. This led to fundamental work on protein structure.

He studied the iodination of insulin and zein, which was affecting the phenolic residues oftyrosine and led to a shift in pKa values of about 3.5. In a paper with Harington (3) heshowed that the derivatized insulin had lost almost all its biological activity and was able todemonstrate the restoration of activity by deiodination. They then studied ultravioletspectroscopy of the proteins in native and denatured states by observing the changes with pH.This was very laborious because at that time only two spectrograms could be done on aprotein in a day. They postulated that hydrogen bonds were largely responsible for the stabilityof native proteins. This was probably the first use of UV spectroscopy for such studies.

Nutritional studies and amino acid metabolism

His interest in nutrition started in 1940 as war work for his first PhD student, Fred Sanger, inwhich they were investigating the nutritional value of the potato proteins, which wasunexpectedly high (6). This led to extensive studies on the metabolism of the essential aminoacid lysine in rats (7). Later, when at the NIMR, he made a particular study of the pathologyresulting from diets deficient in sulphur-containing amino acids. They concluded that thenecrosis of the liver that was seen was due to a decrease in the concentration of liverglutathione (9).

He was involved in many studies of amino-acid metabolism and chemistry, including workwith Arnstein on the feeding of labelled glycine and serine to rats, which established theimportance of the β carbon of serine as a methyl donor via tetrahydrofolate (20), with Elliotton the special nutritional position of threonine (14), with the Cornforths on the metabolismof tryptophan (17, 18) and with Hudson on the stereochemistry of hydroxyproline (8, 10).

At Cambridge, Neuberger had an interest in the chemical modification of particularamino acids in insulin using benzene sulphonyl chloride. Although he did not take thisfurther, it did encourage Sanger to develop fluorodinitrobenzene independently as an end-group reagent. Sanger (1988) said of him:

I knew him best in the 1940s when I became his first PhD student, and I have always felt grateful forall he did for me at that critical time in my career. Not only did he teach me a lot of biochemistry,but—more important still—he taught me how to do research.

Protein metabolism

With the availability of radioisotopes after World War II, the possibilities for metabolicturnover studies increased enormously and Neuberger was one of the first to recognize thispotential. Before radioisotopes were available, the concept of turnover was not considered tobe of importance by most biochemists. He said that although the turnover of proteins inorgans such as the liver and kidney had been recognized, the turnover of structural proteinssuch as collagen had not been investigated. The work of his group at the NIMR showed that




collagen did indeed turn over by a method in which the turnover was measured not by the rateof incorporation of labelled glycine but by the rate of its disappearance from the tissues.From this they found that the rate of turnover varied considerably between liver, skin, boneand tendon. They found that the slowest turnover was in the collagen of the rat tail. This ledthem into the general field of collagen metabolism and they found by the use of isotopes thatthere are soluble precursors of collagen, which are later converted into the insoluble fibres(11, 13, 15, 19).

Having obtained a mass spectrometer at the NIMR, they were able to use the stableisotope 15N. This was administered in labelled yeast protein and demonstrated the high rate ofbreakdown into ammonia and yeast. However, the most important use of the radioactive andstable amino acids was in studies of porphyrin biosynthesis.

Porphyrin biosynthesis

During 1946 and 1947, because of the recent availability of isotopes (both radioactive andstable), Neuberger started to study porphyrin biosynthesis, an area in which his group mademany significant contributions. Porphyrins are of considerable importance in a variety ofareas of biochemistry and medicine because they are the precursors of haem (conjugated withproteins to form haemoglobins, myoglobins, cytochromes and catalases), chlorophylls andcobalamin (vitamin B12). He had been impressed by papers of Shemin & Rittenberg (1946a,b)in which they indicated that the nitrogen atoms of glycine were the precursors of at least someof the nitrogen atoms of protoporphyrin. (The work of Neuberger’s group for several yearsran in parallel with Shemin’s group in New York.) In collaboration with Helen Muir (F.R.S.1977), they synthesized [15N]glycine and [15N]ethanolamine and showed that all four nitrogenatoms of protoporphyrin are derived specifically from glycine and not from ethanolamine(12). They also showed that the carboxyl carbon of glycine was lost in the conversion of thisamino acid to protoporphyrin but that each pyrrolic ring of the porphyrin contained onecarbon atom derived from the α-carbon of glycine. The latter also provided the four methynebridges linking the four pyrrolic rings (16).

Another problem that was addressed was of the intermediates and other precursors ofprotoporphyrin. δ-Aminolaevulinic acid labelled with 14C was synthesized by Scott (21, 22).This was used to investigate the complex pathway from porphobilinogen to protoporphyrin.Eventually the whole pathway from the condensation of glycine and succinyl-CoA, via δ-aminolaevulinic acid to protoporphyrin, was unambiguously demonstrated in a series ofpapers by the groups of Neuberger (23, 24) and of Shemin (Shemin & Russell 1953). Theyhad also discovered the origin of all the carbon and nitrogen atoms of protoporphyrin.

His group extended studies of porphyrin metabolism in the following 20 years. Theyinvestigated congenital and also acute intermittent porphyria, the disorder that caused theapparent ‘madness’ of King George III. By the administration of 15N glycine to normal andporphyric individuals they were able to demonstrate the differences in the metabolism of theporphyrins that later led to other workers’ finding that the disorder was due to a defectiveporphobilinogen deaminase.

Neuberger’s group continued their studies of porphyrin formation in the purplephotosynthetic bacterium Rhodopseudomonas spheroides. This organism was obviously mucheasier to use for metabolic studies than plants or animals, because cultures grow rapidly andcan grow anaerobically in light or aerobically in both light and dark. It also had theadvantage that it produced all three classes of tetrapyrrole, namely bacteriochlorophyll, haem




and vitamin B12. With this bacterium it was possible to study the enzymes involved in thebiosynthesis of haem and bacteriochlorophyll and to demonstrate which enzymes wereactivated or deactivated by light, oxygen and the state of the electron transport chain (29–31, 37, 38).

G

In 1990, Neuberger (55) gave his reasons for being involved in other activities:

I have always felt that an academic scientist is in a privileged position in that he is paid for doingexactly what he wants to do, and this I believe imposes a duty and a responsibility to give some of histime to work which might be beneficial to society as a whole or to other scientists and academiccolleagues. I felt this particularly when I was engaged in full-time research with little or no teaching.

His influence on British science extended well beyond his own considerable researchcontributions, because he was involved in many areas of the management of science. He was,at one time or another, a member of the Medical Research Council (MRC), the AgriculturalResearch Council (ARC), the Council of Scientific Policy, the joint MRC/ARC Committee onFood and Nutrition (of which he was Chairman) and the Independent Committee onSmoking and Health, and he was Royal Society Scientific Governor of the British NutritionFoundation and later Honorary President of the Foundation.

He was also deeply involved with the Lister Institute of Preventive Medicine. From 1968he was a member of the governing body and from 1971 its Chairman. The institute, whichhad a distinguished record in the biomedical field, was loosely connected to the University ofLondon but relied for most of its income on vaccine production at Elstree. In the mid-1970s itbecame apparent that the financial situation was deteriorating. With considerable skill andtact, Neuberger and the committee managed to relocate staff, dispose of the buildings inElstree and Chelsea and produce a considerable capital sum. This was used to set up a trustfund to endow fellowships in the biomedical field. These Lister Fellowships have attractedapplicants of high quality and are yet another example of his foresight.

A I I

In 1945 he spent four months as a consultant in nutrition to the medical directorate of theBritish Army in India, which he said was one of the most interesting experiences of his life.He became very interested in Indian civilization and culture and realized that the nutritionalproblems could not be understood without reference to the whole cultural and socialsituation. He revisited India for two lengthy visits in 1968 and in 1977–78 to advise the IndianMRC and the Nutrition Foundation of India on a variety of research activities.

After a visit in 1950 to the Weizmann Institute in Rehovot he became greatly involved inthe academic life of Israel. At the Weizmann there were collaborations because of a sharedinterest in the biochemistry of carbohydrates. He also became a governor of the HebrewUniversity of Jerusalem and served as Chairman of the Academic Committee of the Board ofGovernors; he valued his contact with the other faculties of the Hebrew University. Heenjoyed visiting Israel particularly because he had retained a knowledge of Hebrew fromchildhood. He and his wife had a flat in Jerusalem and were there frequently.




E

In 1947 he joined the board of the Biochemical Journal and in 1952 became Chairman. Thisinvolved a very heavy workload because he had to read the proofs of almost every paper thatappeared in the journal. He also served on the committee of the Biochemical Society and wasfor two years chairman of the committee. He was elected an Honorary Member of theBiochemical Society in 1973.

In 1968 he joined the editorial board of Biochimica et Biophysica Acta and for much ofthat time was Associate Managing Editor. He was also heavily involved in a series ofmonographs entitled Frontiers of Biology (North-Holland Research Monographs) and in thegeneral editing and planning of the Comprehensive Biochemistry series.

E

Albert Neuberger was an outstanding scientist with an impressive intellect and a range ofinterests outside science. He was very well liked and respected by his colleagues for histolerance, good humour and high scientific standards. He was also a devoted family man andleaves a widow, Lilian, and four sons, one of whom, Michael, is a distinguished molecularbiologist and like his father is a Fellow of The Royal Society.

A

We are very grateful to Mrs Lilian Neuberger, Dr Michael Neuberger and Dr George Tait for their help and fortheir corrections to this text. We have also made extensive use of a Biochemical Society Archive video ofAlbert Neuberger in conversation with Robin Marshall and George Tait.

The frontispiece photograph was taken in 1961 by Godfrey Argent and is reproduced with permission.

R

Irvine, J.C. & Hynd, A. 1912 The conversion of d-glucosamine to d-glucose. J. Chem. Soc. 101, 1128–1146.Irvine, J.C., McNicoll, D. & Hynd, A. 1911 New derivation of d-glucosamine. J. Chem. Soc. 99, 250–261.Perry, S.V. 1987 Rodney Robert Porter. Biog. Mems Fell. R. Soc. Lond. 33, 443–489.Sanger, F. 1988 Sequences, sequences and sequences. A. Rev. Biochem. 57, 1–28.Shemin, D. & Rittenberg, D. 1946a The biological utilization of glycine for the synthesis of the protoporphyrin

of hemoglobin. J. Biol Chem. 166, 621–625.Shemin, D. & Rittenberg, D. 1946b The life span of the human red blood cell. J. Biol. Chem. 166, 627–636.Shemin, D. & Russell, C.S. 1953 δ-Aminolevulinic acid, its role in the biosynthesis of porphyrins and purines.

J. Am. Chem. Soc. 75, 4873–4874.Tamm, I. & Horsfall, F.J. 1950 Characterization and separation of an inhibitor of viral hemagglutinin present

in urine. Proc. Soc. Exp. Biol. Med. 74, 108–114.




B

The following publications are those referred to directly in the text. A full bibliographyappears on the accompanying microfiche, numbered as in the second column. A photocopy isavailable from the Royal Society Library at cost.(1) (1) 1931 (With H. Reinwein) Untersuchungen über die Latenzzeit bei der Autolyse. Biochem. Z.

243, 225–235.(2) (2) Über die Latenzzeit der Autolyse von Hungertieren. Biochem. Z. 243, 236–240.(3) (5) 1936 (With C.R. Harington) Electrometric titration of insulin. Preparation and properties of

iodinated insulin. Biochem. J. 30, 809–820.(4) (11) 1938 Carbohydrates in proteins. 1. The carbohydrate component of crystalline egg albumin.

Biochem. J. 32, 1435–1451.(5) (18) 1940 A new chemical proof of the cyclic structure of glucosaminides. J. Chem. Soc. Lond. 5,

29–32.(6) (23) 1942 (With F. Sanger) The nitrogen of the potato. Biochem. J. 36, 662–671.(7) (27) 1943 (With F. Sanger) The availability of the acetyl derivatives of lysine for growth. Biochem.

J. 37, 515–518.(8) (33) 1945 The stereochemistry of hydroxyproline. J. Chem. Soc. Lond. 107, 429–432.(9) (37) (With L.E. Glynn & H.P. Himsworth) Pathological states due to deficiency of the

sulphur-containing amino-acids. Br. J. Exp. Pathol. 26, 326–337.(10) (46) 1948 Stereochemistry of amino acids. Adv. Protein Chem. 4, 297–383.(11) (47) Amino acids in nutrition. Br. Med. Bull. 5, 346–349.(12) (50) 1949 (With H.M. Muir) The biogenesis of porphyrins. 1. The distribution of 15N in the ring

system. Biochem. J. 45, 163–170.(13) (51) Metabolism of proteins and amino acids. A. Rev. Biochem. 18, 243–266.(14) (54) 1950 (With D.F. Elliott) The irreversibility of the deamination of threonine in the rabbit and

rat. Biochem. J. 46, 207–210.(15) (56) Properties of proteins. J. Sci. Fd Agric., no. 3, 80–83.(16) (61) (With H.M. Muir) The biogenesis of porphyrins. 2. The origin of the methyne carbon

atoms. Biochem. J. 47, 97–104.(17) (64) 1951 (With J.W. Cornforth, R.H. Cornforth & C.E. Dalgleish) -β-3-Oxindolylalanine (-

hydroxytryptophan). 1. Synthesis. Biochem. J. 48, 591–597.(18) (65) (With J.W. Cornforth & C.E. Dalgleish) β-3-Oxoindolylalanine (hydroxytryptophan). 2.

Spectroscopic and chromatographic properties. Biochem. J. 48, 598–603.(19) (73) 1952 Protein metabolism. Br. Med. Bull. 8 (2–3), 210–212.(20) (81) 1953 (With H.R.V. Arnstein) The synthesis of glycine and serine by the rat. Biochem. J. 55,

271–280.(21) (83) (With J.J. Scott) Aminolaevulinic acid and porphyrin biosynthesis. Nature 172, 1093–

1094.(22) (86) 1954 (With J.J. Scott) The synthesis of δ-succinamidolaevulinic acid and related compounds. J.

Chem. Soc. Lond., 1820–1825.(23) (101) 1958 (With W.G. Laver & S. Udenfriend) Initial stages in the biosynthesis of porphyrins. 1.

The formation of δ-aminolaevulic acid by particles obtained from chicken erythrocytes.Biochem. J. 70, 4–14.

(24) (102) (With K.D. Gibson & W.G. Laver) Initial stages in the biosynthesis of porphyrins. 2. Theformation of δ-aminolaevulic acid from glycine and succinyl-coenzyme A by particlesfrom chicken erythrocytes. Biochem. J. 70, 71–81.

(25) (103) (With P. Johansen & R.D. Marshall) Carbohydrate peptide complex from egg albumin.Nature 181, 1345–1346.

(26) (111) 1960 (With P.G. Johansen & R.D. Marshall) Carbohydrates in protein. 2. The hexose,hexosamine, acetyl and amide-nitrogen content of hen’s egg albumin. Biochem. J. 77,239–247.




(27) (119) 1961 (With P.G. Johansen & R.D. Marshall) Carbohydrates in protein. 3. The preparation andsome properties of a glycopeptide from hen’s egg albumin. Biochem. J. 78, 518–527.

(28) (123) (With G.S. Marks) Synthetic studies relating to the carbohydrate–protein linkage in eggalbumin. J. Chem. Soc. Lond., 4872–4879.

(29) (127) 1962 (With K.D. Gibson & G.H. Tait) Studies on the biosynthesis of porphyrin andbacteriochlorophyll by Rhodopseudomonas spheroides. 1. The effect of growth conditions.Biochem. J. 83, 539–549.

(30) (128) (With K.D. Gibson & G.H. Tait) Studies on the biosynthesis of porphyrin andbacteriochlorophyll by Rhodopseudomonas spheroides. 2. The effects of ethionine andthreonine. Biochem. J. 83, 550–559.

(31) (129) (With G.H. Tait) Production of aminoacetone by Rhodopseudomonas spheroides.Biochem. J. 84, 317–328.

(32) (131) (With G.S. Marks & R.D. Marshall) Periodate oxidation of a purified glycopeptidefraction from egg albumin. Biochem. J. 84, 30–31.

(33) (132) (With G.S. Marks & R.D. Marshall) Observations on the carbohydrate–protein bond inegg albumin. Biochem. J. 85, 15–16.

(34) (134) (With G.S. Marks, R.D. Marshall & H. Papkoff) A simplified procedure for the isolationof glycopeptides from glycoproteins. Biochim. Biophys. Acta 63, 340–342.

(35) (136) 1963 (With A.P. Fletcher, G.S. Marks & R.D. Marshall) Carbohydrates in protein. 5.Procedures for the Isolation of glycopeptides from hen’s egg albumin and their oxidationby periodate. Biochem. J. 87, 265–273.

(36) (137) (With G.S. Marks & R.D. Marshall) Carbohydrates in protein. 6. Studies on thecarbohydrate–peptide bond in hen’s egg albumin. Biochem. J. 87, 274–281.

(37) (142) (With K.D. Gibson & G.H. Tait) Studies on the biosynthesis of porphyrin andbacteriochlorophyll by Rhodopseudomonas spheroides. 4. S-Adenosylmethionemagnesium protoporphyrin methyltransferase. Biochem. J. 88, 325–334.

(38) (146) 1964 (With G.H. Tait) Studies on the biosynthesis of porphyrin and bacteriochlorophyll byRhodopseudomonas spheroides. 5. Zinc-protoporphyrin chelatase. Biochem. J. 90, 607–616.

(39) (147) (With R.D. Marshall) Carbohydrates in protein. VIII. The isolation of 2-acetamido-1-(-β-aspartamido)-1,2-dideoxy-β--glucose from hen’s egg albumin. Biochemistry 3, 1596–1600.

(40) (174) 1970 (With A.P. Fletcher & W.A. Ratcliffe) Tamm–Horsfall urinary glycoprotein. Thechemical composition. Biochem. J. 120, 417–424.

(41) (175) (With A.P. Fletcher & W.A. Ratcliffe) Tamm–Horsfall urinary glycoprotein. The subunitstructure. Biochem. J. 120, 425–432.

(42) (179) 1971 (With A.M.S. Marr & W.A. Ratcliff) Rabbit Tamm–Horsfall urinary glycoprotein.Chemical composition and subunit structure. Biochem. J. 122, 623–631.

(43) (181) Past and present concepts of glycoproteins. In Glycoproteins of blood cells and plasma

(4th Ann. Sci. Symp., American National Red Cross) (ed. G.A. Jamieson &T.J. Greenwalt), pp. 1–15. Philadelphia: Lippincott.

(44) (186) 1973 (With A.K. Allen & N. Sharon) The purification, composition and specificity of wheat-germ agglutinin. Biochem. J. 131, 155–162.

(45) (193) (With A.K. Allen) The purification and properties of the lectin from potato tubers, ahydroxyproline-containing glycoprotein. Biochem. J. 135, 307–314.

(46) (209) 1976 (With A.K. Allen & N.N. Desai) The purification of the glycoprotein lectin from thebroad bean (Vicia faba) and a comparison of its properties with lectins of similarspecificity. Biochem. J. 155, 127–135.

(47) (218) 1978 (With A.K. Allen & N.N. Desai) Properties of potato lectin and the nature of itsglycoprotein linkages. Biochem. J. 171, 665–674.

(48) (223) 1980 (With D. Ashford) 4-hydroxy--proline in plant glycoproteins. Trends Biochem. Sci. 5,245–248.




(49) (225) 1981 (With N.N. Desai & A.K. Allen) Some properties of the lectin from Datura stramonium

(thorn-apple) and the nature of its glycoprotein linkages. Biochem. J. 197, 345–353.(50) (227) 1981 (With D. Ashford, R. Menon & A.K. Allen) Studies on the chemical modification of

potato (Solanum tuberosum) lectin and its effect on haemagglutinating activity. Biochem.J. 199, 399–408.

(51) (228) 1982 (With D. Ashford, N.N. Desai, A.K. Allen, M.A. O’Neil & R.R. Selvendran) Structuralstudies of the carbohydrate moieties of lectins from potato (Solanum tuberosum) tubersand thorn apple (Datura stramonium) seeds. Biochem. J. 201, 199–208.

(52) (229) (With D. Ashford & A.K. Allen) The production and properties of an antiserum topotato (Solanum tuberosum) lectin. Biochem. J. 201, 641–645.

(53) (232) 1983 (With N.N. Desai & A.K. Allen) The properties of potato (Solanum tuberosum) lectinafter deglycosylation by trifluoromethanesulphonic acid. Biochem. J. 211, 273–276.

(54) (238) 1986 (With G.-J. Van Holst, S.R. Martin, A.K. Allen, D. Ashford & N.N. Desai) Proteinconformation of potato (Solanum tuberosum) lectin determined by circular dichroism.Biochem. J. 233, 731–736.

(55) (243) 1990 Neuberger, A. An octogenarian looks back. In Comprehensive biochemistry (ed.G. Semenza & R. Jaenicke), vol. 37, pp. 21–65. Amsterdam: Elsevier Science Publishers.



Albert Neuberger. 15 April 1908 −− 14 August 1996: Elected ...rsbm.royalsocietypublishing.org/content/roybiogmem/47/369.full.pdf · Albert Neuberger. 15 April 1908 −− 14 ...

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