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Mixture of protein digesting enzymes known as proteolytic
enzymes or proteases include several other substances as welleither
of two proteases extracted from plant family bromeliaceae i.e.,
Stem bromelain - EC 3.4.22.32 Fruit bromelain - EC 3.4.22.33May
also refer to a combination of those enzymes along with other
compounds produced in an extractReferred to as sulfhydryl proteases
since a free sulfhydral group of a cysteine side chain is
essentialThe other substances typically include peroxidase, acid
phosphatase, protease inhibitors, and calcium
WHAT ACTUALLY IS BROMELAIN??
temperature 40-60 COptimal temperature 50-60 CDeactivation
temperature above65 C approx.Effective pH 4.0-8.0Optimal pH
4.5-5.5Molecular weight 28.4 kD
COILS HELIXES AND HELICAL TURNS The term "bromelain" can refer
to either of two protease enzymes extracted from the plant family
Bromeliaceae, or it can refer to a combination of those enzymes
along with other compounds produced in an extract.
1PEEK IN TO THE PASTFirst isolation Vicente Marcano in 1891 from
fruit of pineapple.In 1892, Chittenden, Joslin and Meara
investigated the matter fully and named it BromelinLater, Bromelian
was introduced and orignally applied to any protease from any
member of family Bromeliaceae.In 1957 first introduced as
therapeutic supplementPioneer research at Hawaii but recent in
countries in Asia, Europe and Latin America. Germany has recently
taken a great interest in bromelian research.13th most widely used
herbal medicine in Germany.
2IT COMES FROMPineapple plant (Ananas sp.)Stem most common
commercial sourceTraditionally as a medicinal plant among natives
of South and Central America.Produced in Thailand, Taiwan, and
other tropical parts of the world where pineapples are
grown.Prepared from stem part of pineapple after harvesting the
fruit.
Bromelain is present in all parts of the pineapple plant (Ananas
sp.) However, the stem is the most common commercial source,
presumably because it is readily available after the fruit has been
harvested. Pineapples have had a long tradition as a medicinal
plant among the natives of South and Central America.It is produced
in Thailand, Taiwan, and other tropical parts of the world where
pineapples are grown.
Bromelain is prepared from the stem part of the pineapple plant
after harvesting the fruit. This stem part is peeled, crushed, and
pressed to get the juice containing the soluble bromelain enzyme.
Further processing includes purification and concentration of the
enzyme
3ROLE OF THE STUDBromelain bloods fibrolytic activity and
kininogen and bradykinin serum and tissue levels as well as reduce
excretion of proinflammatory cytokines and chemokinesAlso effects
prostaglandin synthesisInhibits fibrinogen synthesisDirectly
degrades fibrin and fibrinogencleave at Lys-, Ala-, Tyr-, Gly- Is
activated by cysteine, bisulfite salt, NaCN, H2S, Na2S, and
benzoate.inhibited by Hg++, Ag+, Cu++, a-1-antitrypsin, estatin
A&B, Iodoacetate, TLCK, TPCK
Bromelain, increases blood fibrinolytic activity as well as
inhibiting fibrinogen synthesis; bromelain also directly degrades
fibrin and fibrinogen. Kininogen and bradykinin serum and tissue
levels are lowered by bromelain and it also affects prostaglandin
synthesis, which gives it's antiinflammatory effects. Bromelain has
been found to reduce the excretion of proinflammatory cytokines as
well as chemokines in a study into its possible mechanism of action
in ulcerative colitis, inflammatory bowel disease, Crohn's
disease
4PAY BACK TIMEproduct name AnanaseVarious uses in Folk
medicineExplored as a potential healing agent in alternative
medicine. Work by blocking some proinflammatory metabolites when
applied topicallyUsed for reducing swellingInvolved in the
migration of neutrophils to the site of acute inflammation. Used
for treating arthiritisWhen used in conjunction with trypsin and
rutin is as effective as prescribed analgesics in the
osteoarthiritis management.Meat tenderizing
Available in some countries as a product under the name
'Ananase', bromelain began its reputation for various uses in folk
medicine and continues to be explored as a potential healing agent
in alternative medicine. First introduced in medical research in
1957, bromelain may work by blocking some proinflammatory
metabolites when applied topically. Bromelain may be used after
surgery to reduce swelling. Preliminary research indicates that
bromelain may affect migration of neutrophils to sites of acute
inflammation. As a potential anti-inflammatory agent, it may be
useful for treating arthritis, but has neither been confirmed in
human studies for this use nor is it approved with a health claim
for such an effect by the Food and Drug Administration or European
Food Safety Authority. The Natural Medicines Comprehensive Database
suggests that bromelain, when used in conjunction with trypsin and
rutin is as effective as some prescription analgesics in the
management of osteoarthritis.
5WHAT ELSE??Other effects include: Hay feverTreating a bowel
condition that includes swelling and ulcer ulcerative
colitisRemoving dead and damaged tissue after a burn
debridementPreventing the collection of water in the lung pulmonary
edemaRelaxing musclesImproving the absorption of
antibioticsPreventing cancer Shortening laborHelp the body in
reducing fatsSupplement may effect heart ratesystemic enzyme
therapy
Bromelain may also be used for a variety of other effects that
remain scientifically unconfirmed and not authorized by regulatory
authorities like the Food and Drug Administration. Systemic enzyme
therapy (consisting of combinations of proteolytic enzymes such as
bromelain, trypsin, chymotrypsin, and papain) has been investigated
in Europe to evaluate the efficacy of proteolytic enzymes in the
treatment of breast, colorectal, and plasmacytoma cancer patients.
In mice with experimental colitis, 6 months of dietary bromelain
from pineapple stem or from fresh juice decreased the severity of
colonic inflammation and reduced the number of cancerous lesions in
the colon.
6DIASTASE Diastase are any one of a group of enzymes which
catalyses the breakdown of starch into maltose.first enzyme
discovered. It was extracted from malt solution in 1833 by Anselme
Payen and Jean-Franois Persoz, chemists at a French sugar
factory.The name "diastase" comes from the Greek (diastasis) (a
parting, a separation)
because when beer mash is heated, the enzyme causes the starch
in the barley seed to transform quickly into soluble sugars and
hence the husk to separate from the rest of the seed.[4][5] 7ALPHA
AMYLASEEC NUMBER: 3.2.1.1 is 1,4-a-D-Glucan
glucanohydrolaseALTERNATIVE NAME : glucogenaseLocation: it is
secreted in saliva and pancreas, found in humans and other animals
food reserve of fungi/Acts on starch, glycogen and related
polysaccharides and oligosaccharides in a random manner; reducing
groups are liberated in the alpha-configuration.Causes hydrolyses
alpha-bonds of large alpha-linked polysaccharides, such as starch
and glycogen, yielding glucose and maltose.
STRUCTURE 679 amino acid residues with a molecular weight of
75112 residuesIt has 3 domains A B CDOMAIN A: These domains are
generally found on all -amylase enzymes. The A domain constitutes
the core structure, with a (/)8-barrel. DOMAIN B :consists of a
sheet of four anti-parallel -strands with a pair of anti-parallel
-strands. Long loops are observed between the -strands. Located
within the B domain is the binding site for Ca2+-Na+-Ca2+. DOMAIN C
consisting of eight -strands is assembled into a globular unit
forming a Greek key motif. It also holds the third Ca2+ binding
site in association with domain AACTIVE SITE:Positioned on the
C-terminal side of the -strands of the (/)8-barrel in domain A is
the active site. The catalytic residues involved for the BSTA
active site are Asp234, Glu264, and Asp331
AMYLOSE IN STARCH
GLUCOSE RESIDUE CLEAVED BY AMYLASE
MECHANISM OF action of alpha amylose:Alpha amylose converts
amylose or starch to maltose. Alpha-amylase hydrolyzes bonds
between glucose repeats. Starch is a polysachride made up of 2
residues amylose and amylopectin. Alpha amylase is breaks down
starch by hydrolysis to release maltoseThe reaction occurs in 3
steps:The simple glucose molecules have a bond between the 1 carbon
in the ring and the 4 carbon in the ring. They are joined by an
oxygen. AMYLOSEBelow is the building block of starch, glucose.
Notice that when the single oxygen is left in the bond in the
amylose, the two glucose molecules must have lost two hydrogen and
an oxygen in the formation of this bond- or one H2O molecule. This
chemical reaction is called dehydration, because it generates
water.
Similarly, when this bond breaks to generate a free glucose or
pairs of free maltose,there is the addition of a water molecule to
make the OH at carbon 1 and carbon 4. This is called hydrolysis or
Hydro (water) + Lysis (breaking). One of the disaccharides or
monosaccharides gets an OH- from the water molecule and the other
part gets an H+ from the water. Hydration is adding a water without
splitting the molecule apart.10INDUSTRIAL APPLICATION:used in
ethanol production to break starches in grains into fermentable
sugars.detergents, especially dishwashing and starch-removing
detergents.in textile weaving, starch is added for warping.-Amylase
is used for the production of malt, as the enzyme is produced
during the germination of cereal grainsChecking out pancerititis
the amylase levels are measured in the pancertic cells.
11
ENZYME: TRYPSIN*TYRPSINOGEN*HISTORY & SOURCE***1876, first
named by Kuhne who described the proteolytic activity of this
pancreatic enzyme.1931, Norothrop and Kunitz purified trypsin by
crystallization.1974, three dimensional structure was
determined
PancreasTRYPSINOGEN TRYPSIN
Bovine Pancreasexpresses two forms of trypsin:dominant cationic
formminor anionic formThese protein sequences share 72% identity,
while their coding regions share 78%
identity.CONVERSION***TRYPSINOGEN TRYPSIN {Ph 9.3} {ph
10.5}Trypsinogen is activated by removal of a terminal hexapeptide
to yield single-chain -trypsin. Limited autolysis produces other
active forms having two or more peptide chains bound by disulfide
bonds. Predominant forms are *-trypsin, having two peptide chains
and *-, a single chainREACTION CATALYZED***Process catalyzed by
trypsin
*Trypsin Proteolysis* {Trypsinisation}
Trypsin is considered as an endopeptidase* Cleavage occurs
within the polypeptide chain rather than at the terminal amino
acids located at the ends of polypeptides.TRYPSIN
SERINE PROTEASE
HYDROLYZE PROTEINSUSED FOR***Tissue dissociationMitochondria
isolationin vitro studies of proteins Various hemagglutination
proceduresDNA FingerprintingEnvironmental monitoringReduction of
cell density in tissue cultureCleavaging fusion proteinsGenerating
glycopeptides from purified glycoproteins
What is Alkaline Phosphatase?Alkaline phosphatase (EC
3.1.3.1)comprises a group of enzymes that catalyze the hydrolysis
of phosphate esters in an alkaline environment, generating an
organic radical and inorganic phosphate. This has many isoenzymes
includingIntestinal (ALPI), Chromosome 2Placental
(ALPP)Liver/bone/kidney (ALPL) Chromosome 1It belongs to Alpha and
Beta class of proteins
Alkaline phosphatase is pertinent in recycling phosphate within
living cells. Alkaline Phosphatases are a group of enzymes found
primarily the liver (isoenzyme ALP-1) and bone (isoenzyme ALP-2).
There are also small amounts produced by cells lining the
intestines (isoenzyme ALP-3), the placenta, and the kidney (in the
proximal convoluted tubules). The structure of alkaline phosphatase
differs depending on where that particular enzyme originated.
Alkaline phosphatase from bone looks different from alkaline
phosphatase from the liver. These different structures are called
isozymes
17Alkaline phosphatase is a glycoprotein mainly parallel beta
sheets Core has 3 layers: a/b/a.In general, alkaline phosphatase is
a dimer containing nearly identical subunits which each have two
molecules of zinc and one molecule of magnesium ion. One molecule
of zinc is tightly bound, giving the structure stability and the
other is loosely bound which provides for the catalytic
activity.STRUCTURE
General Mechanism
IIIIIIIV19Properties AND FUNCTIONThis enzyme was partially
purified and studied by Kunitz (1960)It is a hydrolase enzyme found
in bacteria and mammals Optimum pH: 8 9Activators: Mg2+Wide
specificityInhibitors: acidic pH, chelators of the metal ions, urea
and high levels of Zn2+The property of dephosphorylation allows for
uses in molecular biology, in pasteurization and in nature by
bacteria.It catalyses the following reactionA phosphate monoester +
H(2)O an alcohol + phosphateElevated levels (five-times higher than
normal) are found in the blood serum of people suffering from
various bone and liver diseases. Irritable bowel syndrome,
germ-cell tumors and liver infections will raise serum levels of
Alkaline Phosphatase to a lesser extent.Alkaline phosphatase (ALP)
is an enzyme normally present in raw milk and it is inactivated
when thermal treatment conditions are slightly higher than those
required for the destruction of the pathogenic bacteria. Hence, the
chemical test carried out to determine alkaline phosphatase (ALP)
concentration in pasteurized milk is used to verify if thermal
treatment has been done correctly. Alkaline phosphatase is useful
in the dairy industry as a marker for successful pasteurization in
cow's milk. At the high temperatures of pasteurization, alkaline
phosphatase is supposed to denature. To test this, experts
sometimes add a para-nitrophenylphosphate substrate to the milk. If
alkaline phosphatase is present, it will break down this phosphate
molecule, causing the milk to change color to yellow. Properly
pasteurized milk will not change cALP activity can be used to
measure the effectiveness of pasteurization.
20One of the most important functions of alkaline phosphatase is
as an indicator for disease.Alkaline Phosphatase TestThe blood
serum level of Alkaline Phosphatase is used as a marker for
disease. Elevated levels (five-times higher than normal) are found
in the blood serum of people suffering from various bone and liver
diseases. Irritable bowel syndrome, germ-cell tumors and liver
infections will raise serum levels of Alkaline Phosphatase to a
lesser extent.
21
PEPSIN ClassificationEC number 3.4.23.3Member of the aspartate
protease family First animal enzyme to be discoveredSecond to be
crystallized
Discovery Theodor Schwann Northrop
22Structure:
Two aspartate molecules at the active site Three sulphide
bridges23 PEPSINOGEN - primary structure has an additional 44 amino
acids Released by chief cells in the stomach HCL causes activation
Pepsinogen pepsin( autocatalysis in acidic env)
A tricky businessTARGETS: Amide bonds of aromatic amino acids
like tryptophan, phenylalanine and tyrosine
Tryptophan Phenylalanine
24Temperature: 37C-42CpH: 1.5 2Stable until pH 8- can be
reactivated upon re- acidificationActivity and Stability:Imbalance
in pHInability to digest proteinDeficiency:25PAPAIN
Papaya Proteinase ICysteine protease hydrolaseEnzyme
extraction
Family & structureSource: present inpapaya(Carica papaya)
andmountain papaya(Vasconcellea cundinamarcensis).Cysteine
protease(EC3.4.22.2)enzymeFamily: members found in
baculovirus,eubacteria, yeast, and practically all protozoa, plants
and mammals, lysosomal or secretedcontains 345 amino acid
residues,and consists of a signal sequence (1-18),
apropeptide(19-133) and the mature peptide (134-345). The amino
acid numbers are based on the mature peptide. The protein is
stabilised by threedisulfide bridges.
Mechanism of actionmechanism by which it breakspeptide
bondsinvolves deprotonation of Cys-25 by His-1591. Deprotonation of
thiol in cysteine by basic histidine2. Nucleophilic attack by
deprotonated cysteine on substrate carbonyl atom
applicationsThe main function of the papain enzyme is to aid in
digestion and to promote effective digestive health. This is done
by breaking down all the protein in the body for easy digestion.The
papain enzyme as a meat tenderizer has been used for many years.
Since it is a proteolytic enzyme that tenderizes meat, it also acts
as a clarifying agent in many food industry processes.It is used in
treatment of stings that are administered by jellyfish, bees, wasps
or insects by breaking down the toxin and the venom.It boosts the
immune system and is seen to be beneficial in food allergies and
tumors
Introduction (Cellulase)
Cellulaserefers to an entourage of enzymes produced chiefly by
fungi, bacteria and protozoans that catalyze cellulolysis (i.e.
thehydrolysisof cellulose). However, there are also cellulases
produced by a few other types of organisms, such as sometermitesand
the microbial intestinal symbionts of other termites.Several
different kinds of cellulases are known, which differ structurally
and mechanistically.Some species of fungi and bacteria are able to
exhaustively digest crystalline cellulose in pure culture are said
to have complete or true cellulases.
The majority of organisms that produce cellulases can only
hydrolyze the cellulose in their diets to certain extent. they are
known as incomplete cellulases.
These cellulases unable to digest cellulose exhaustively can
still generate sufficient amount of glucose for their producers.
Endogenous cellulases of termites belong to this category.
Complete vs. incomplete cellulases32Types of reactions/
Classification
General types of cellulases based on the type of reaction
catalyzed:
Cleaves internal bonds at Endocellulase (EC 3.2.1.4) randomly
amorphous sites that create new chain ends.Cellobiase (EC 3.2.1.21)
orbeta-glucosidase hydrolyses the exocellulase product into
individual monosaccharides.Cellulose phosphorylases depolymerize
cellulose using phosphates instead of water.
Uses
Cellulase is used for commercial food processing incoffee. It
performshydrolysisof cellulose during drying ofbeans.Furthermore,
cellulases are widely used in textile industry and in laundry
detergents. They have also been used in the pulp and paper industry
for various purposes, and they are even used for pharmaceutical
applications. Cellulase is used in the fermentation of biomass
intobio fuels, although this process is relatively experimental at
present. Cellulase is used as a treatment for phytobezoars, a form
of cellulosebezoarsfound in the humanstomach.
34Succinyl coenzyme A synthetase
Succinyl coenzyme A synthetaseis an enzyme thatcatalyzesthe
reversible reaction ofsuccinyl-CoAtosuccinate.Source
Bacteria e.g.E.coli
MammalsChemical ReactionSuccinyl CoA synthetase catalyzes the
followingreversible reaction:
Succinyl CoA + Pi + NDP Succinate + CoA + NTP
Succinyl CoAsuccinate
MechanismThe enzyme facilitates coupling of the conversion of
succinyl CoA to succinate with the formation of NTP from NDP and
Pi. The first step involves displacement ofCoAfrom succinyl CoA by
anucleophilicinorganic phosphate molecule to form succinyl
phosphate. The enzyme then utilizes ahistidineresidue to remove the
phosphate group from succinyl CoA and generate succinate. Finally,
the phosphorylated histidine transfers the phosphate group to a
nucleoside diphosphate, which generates the high-energy carrying
nucleoside triphosphate. Mechanism
UsesSuccinyl-CoA synthetase plays a key role in
the citric acid cycle ketone metabolism heme synthesis
Urokinase sourcesSOURCE ORGANISM
Human urine.much lower concentrations in human plasma. Other
organism may include rat, mouse, yeast etc.
SOURCE TISSUE
Ovaryproduced by kidney cells.produced by a variety of
tumorcells and involved in the formation of
tumormetastasis.Phagocytic cells
Urokinase is found in humanurineand in much lower concentrations
in human plasma. In the body, urokinase is produced by kidney
cells, and its presence in the urine promotes the dissolution of
any bloodclotsin the urine-collecting system of the kidneys or
thebladder. Urokinase is also produced by a variety oftumorcells,
and it is thought to be involved in the formation of
tumormetastases. Urokinase can be inhibited by
plasmainhibitorproteins. The presence of cell receptors and
inhibitors suggests that the regulation of urokinase function is
complex.
Read
more:http://www.answers.com/topic/urokinase#ixzz1qg5lkDNo41
MOLECULAR CHARACTERISTICS411-residue proteinthreedomains: serine
protease domain, kringle domain and growth factor domain.
synthesized as a prourokinase or single-chain urokinase form ;
activated by proteolytic cleavage. The two resulting chains are
kept together by disulphidebond.found in multiple molecular sizes.
Low molecular weight (33-KDa) and high molecular weight (57-KDa).
Urinary Urokinase contained predominantly the LMW formIt was found
that urinary UK contained predominantly the LMW form. It was
suggested that the HMW form is the native structure and that it is
converted to the LMW form by cellular proteases. However, under
certain conditions, HMW form was found to be more active when
assayed with standard enzyme kinetic methods.42
REACTION CATALYSEDPLASMINOGEN + H20 PLASMINSpecific cleavage of
Arg-Val bond in plasminogen to form plasmin.Reaction type:
Hydrolysis of peptide
bondhttp://www.cs.stedwards.edu/chem/Chemistry/CHEM44/serenil/metastasis.html
43
USESused clinically for therapy of thrombotic disordersused in
medicine to dissolve blood clots.employed in clinical medicine in
the treatment ofacute myocardial infarction and arterial blood
clots in the legs and arms.Used in peritoneal dialysis.
LuciferaseSourceLuciferaseis a generic term for the class of
oxidativeenzymes used inbioluminescence62 kDa molecular weightpH
optimum of 7.8A variety of organisms regulate their light
production using different
luciferasesbacteriaFirefliesJack-O-Lantern mushroomMetridia longa
(marine copepod)Dinoflagellate, etc
Luciferase can be produced in the lab throughgenetic
engineeringfor a number of purposes. Luciferasegenescan be
synthesized and inserted into organisms or transfected into
cells.Mice,silkworms, andpotatoesare just a few organisms that have
already been engineered to produce the protein45
Chemical reactionThe chemical reaction catalyzed by firefly
luciferase takes place in two steps:
luciferin+ATPluciferyl adenylate+PPiluciferyl adenylate +
O2oxyluciferin+AMP+ light
Light is emitted because the reaction forms oxyluciferin in an
electronicallyexcited state. The reaction releases a photon of
light as oxyluciferin returns to theground state.46Mechanism
StructureThe protein structure of firefly luciferase consists of
two compactdomain
The N-terminal domainThe C-terminal domain
USESgene report and detectionRNAi system researchinteraction
between proteinscell analysisdetection of Microorganism
Asparaginase
EC 3.-.-.-Hydrolases. [16,495PDB entries]EC 3.5.-.-Acting on
carbon-nitrogen bonds, other than peptide bonds. [1,218PDB
entries]EC 3.5.1.-In linear amides. [444PDB entries]EC
3.5.1.1Asparaginase.[27PDB entries]50About proteinA tetrameric
protein composed of four identical subunits, each subunit contains
326 amino acid residues. The two threonine residues present at the
active site are required for activity.Molecular Weight:Monomer:
36.8 kDa Optimal pH:8.0- 8.6
ADVANTAGESTreatment of acute lymphoplastic leukemia.Aspariginase
can be used as a food processing aid to reduce the formation of
acrylamide, a suspected carcinogen, in starchy food products.
DISADVANTAGESanaphylaxispancreatitis coagulopathy
Mechanism of action as a food processing aidAspariginase can be
used as a food processing aid to reduce the formation of
acrylamide, a suspected carcinogen, in starchy food products.
Acrylamide is a chemical compound that is formed in starchy foods
when they are baked or fried. During heating theamino
acidasparagine, naturally present in starchy foods, is converted
into acrylamide in a process called theMaillard reaction. The
reaction is responsible for giving baked or fried foods their brown
color, crust and toasted flavor.By adding asparaginase before
baking or frying the food, asparagine is converted into another
common amino acid,aspartic acid, andammonium. As a result,
asparagine cannot take part in the Maillard reaction, and therefore
the formation of acrylamide is significantly reduced. Complete
acrylamide removal is probably not possible due to other, minor
asparagine-independent formation pathways[1].As a food processing
aid, asparaginases can effectively reduce the level of acrylamide
up to 90% in a range of starchy foods without changing the taste
and appearance of the end product[4].[edit]Mechanism of action as a
drugThe rationale behind asparaginase is that it takes advantage of
the fact that ALL leukemic cells are unable to synthesize the
non-essential amino acid asparagine, whereas normal cells are able
to make their own asparagine; thus leukemic cells require high
amount of asparagine. These leukemic cells depend on circulating
asparagine. Asparaginase, however, catalyzes the conversion
ofL-asparagine to aspartic acid and ammonia. This deprives the
leukemic cell of circulating asparagine.The mainside effectis
anallergicor hypersensitivity reaction;Asparaginase has also been
associated withpancreatitis. Additionally, it can also be
associated with a coagulopathyas it decreases protein synthesis,
including synthesis of coagulation factors (eg progressive isolated
decrease offibrinogen) and anticoagulant factor
(generallyantithrombinIII; sometimesprotein C&Sas well),
leading tobleedingorthrombotic eventssuch as stroke.
Anaphylaxisis defined as "a seriousallergic reactionthat is
rapid in onset and may cause death".[1]It typically results in a
number of symptoms including an itchy rash, throat swelling, and
lowblood pressure. Common causes include insect bites, foods, and
medications.Pancreatitisisinflammationof thepancreas. It occurs
when pancreatic enzymes (especiallytrypsin) that digest food are
activated in the pancreas instead of the small intestine. It may
beacute beginning suddenly and lasting a few days, orchronic
occurring over many years. It has multiple causes and
symptoms.Coagulopathy(also calledclotting disorderandbleeding
disorder) is a condition in which the bloods ability to clot is
impaired. This condition can cause prolonged or excessive bleeding,
which may occur spontaneously or following an injury or medical and
dental procedures.
52
POTENTIALfusion protein of asparaginase-TTP-CETPC could also be
useful for the development of a vaccine against
atherosclerosis.