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Trypsin trypsinization

Protein digestion occurs in two stages endopeptidases catalyse the hydrolysis of peptide bonds within the protein molecule to form peptides, and the peptides are hydrolysed to form the amino acids by exopeptidases and dipeptidases. Enteropeptidase initiates pro-enzyme activation in the small intestine by catalysing the conversion of trypsinogen into trypsin. Trypsin is able to achieve further activation of trypsinogen, i.e. an autocatalytic process, and also activates chymotrypsinogen and pro-elastase, by the selective hydro-... [Pg.80]

Two-dimensional electrophoresis [86] is a well established technique for the separation of intact proteins. In the first dimension the proteins are separated based on their isolectric point while the second dimension separates them based on their size. The presence on the gel of the proteins is revealed by Coomassie blue or silver staining. Under favorable conditions several thousand spots can be differentiated. The gel is digitized and computer-assisted analysis of the protein spot is performed. The spots of interest are excised either manually or automatically and then digested with trypsin. Trypsin cleaves proteins at the C-terminal side of lysine and arginine. In general one spot represents one protein and the peptides are analyzed by MALDI-TOF to obtain a peptide mass fingerprint. A peptide mass fingerprint involves the determination of the masses of all pep-... [Pg.50]

A different case occurs for the trypsin-trypsin inhibitor complex, where protein steric strain occurs in the free inhibitor. [Pg.92]

Trypsin is the most frequently used serine protease. Generally, porcine or bovine pancrease is used as the source of pure trypsin. Trypsin usually digests proteins at their lysine and arginine residues. The superiority of trypsin is that it displays good activity both in solution and in-gel digestion protocols. [Pg.106]

Figure 4.24. Cleavage by Trypsin. Trypsin hydrolyzes polypeptides on the carboxyl side of arginine and lysine residues. Figure 4.24. Cleavage by Trypsin. Trypsin hydrolyzes polypeptides on the carboxyl side of arginine and lysine residues.
It is a proteolytic enzyme, present in the intestine in its inactive form (zymogen), trypsinogen. Trypsinogen is converted into its active form, trypsin, by enteropeptidase, a specialized proteolytic enzyme secreted by intestinal cells. Some free trypsin formed also catalyses the conversion of trypsinogen into trypsin. Trypsin can also convert chymotrypsinogen and procarboxypeptidase into chymotrypsin and carboxypeptidase, respectively. Trypsin has different amino acid specificity when compared with other proteolytic enzymes. Trypsin hydrolyses those peptide bonds whose carboxyl groups are contributed by Lys or Arg residues and if the next residue is not proline. The number of smaller peptides resulting from trypsin action is equal to the total number of Arg and Lys residues in the protein plus one. [Pg.428]

Trypsin Trypsin crystallized Proteolytic enzyme Aerosol. 125.000 ... [Pg.839]

Figure 8. Stereoview of trypsin + trypsin inhibitor showing backbone atoms. This model shows the separated enzyme + inhibitor prior to formation of the... Figure 8. Stereoview of trypsin + trypsin inhibitor showing backbone atoms. This model shows the separated enzyme + inhibitor prior to formation of the...
Trypsin Trypsin yields the same type of fragments... [Pg.120]

Quantum mechanical and semi-empiiical calculations support this suggestion. For example, it has been shown that, contrary to earlier suggestions, lysozyme does not distort the chair conformation of polysaccharide pyranoside units [32]. Similarly, it has been suggested that the serine proteases distort the trigonal planar arrangement around the carbonyl carbon of amides and peptides (XVII) to a non-planar conformation which resembles the tetrahedral intermediate (XVIII). Support for this hypothesis came from X-ray studies of the trypsin-trypsin inhibitor complex [33]. [Pg.49]

The low pH of the stomach contents stimulates the secretion of the hormone secretin, as it passes into the small intestine. This hormone is secreted into the bloodstream, and when it reaches the pancreas, it stimulates that organ to secrete bicarbonate into the gut which neutralizes the low pH of the entering stomach contents. Entering amino acids stimulate the secretion by intestinal cells of the specialized enzyme enterokinase. It specificity is directed toward the conversion of the zymogen, trypsinogen, secreted by the pancreas, to the active proteolytic enzyme, trypsin. Trypsin then converts chymotrypsinogen to the active chymotrypsin. These two enzymes reduce polypeptides to small peptides. The further hydrolysis of the small peptides to their constituent amino acids is accomplished by two other enzymes secreted by intestinal cells, carboxypeptidase and aminopeptidase. The mixture of amino acids is then transported across the intestinal cells, enters the blood, and is transported to the liver. [Pg.478]

Janin, J., and Chothia, C. (1976). Stability and specificity of protein-protein interactions The case of the trypsin-trypsin inhibitor complexes./. Mol. Biol. 100, 197-211. [Pg.69]

Trypsin Trypsin 1 75 Trypsin 1 80 Trypsin 1 150 232-655-5 Uricase Uricase S 232-656-0 Urease 232-658-1 Agar... [Pg.6901]

Figure 3. MnClj inhibition of DPC -> DCIP activity of Tris- (control, O), then trypsin-treated control PS II membranes. Membranes were treated with trypsin ( ), trypsin and EDC (A), or carboxypeptidase A and trypsin (O). Figure 3. MnClj inhibition of DPC -> DCIP activity of Tris- (control, O), then trypsin-treated control PS II membranes. Membranes were treated with trypsin ( ), trypsin and EDC (A), or carboxypeptidase A and trypsin (O).
Hgure 2 Percentage metal extracted, relative to the total concentration, from marine sediments by different reagents, enzymes, and the gut fluid from cod. HCI = 1 mol I HCI HOAc=25% glacial acetic acid NaOH =0.1 mol I NaOH Pepsin = Pepsin A pH 2 Trypsin = Trypsin ll-S pH 7.6 Gut fluid (1) = natural filtered intestinal fluid, pH 7 Gut fluid (2) = natural filtered intestinal fluid, pH 2. (A) Cu and (B) Zn. (Adapted from Turner A and Olsen YS (2000) Chemical versus enzymatic digestion of contaminated estuarine sediment Relative importance of iron and manganese oxides in controlling trace metal bioavailability. Estuarine, Coastal and Shelf Science 51 717-728.)... [Pg.1996]

In adipose tissues, insulin accelerates the dissimilation of glucose to CO2 through the Embden-Meyerhof pathway and the hexose monophosphate shunt and increases its utilization for glycogen and fatty acid synthesis. Insulin is without effect on fatty acid uptake and lipogenesis when glucose is absent from the medium. And the studies of Fain and Loken [132] have established that the antilipolytic effect of insulin is blocked by trypsin. Trypsin does not affect its inhibition through other metabolic interferences. A protein factor, possibly a receptor, probably is needed for insulin s action on adipose tissue. [Pg.520]


See other pages where Trypsin trypsinization is mentioned: [Pg.12]    [Pg.337]    [Pg.521]    [Pg.181]    [Pg.78]    [Pg.267]    [Pg.157]    [Pg.68]    [Pg.167]    [Pg.97]    [Pg.298]    [Pg.189]    [Pg.1855]    [Pg.120]    [Pg.609]    [Pg.83]    [Pg.646]    [Pg.688]    [Pg.507]    [Pg.319]    [Pg.342]    [Pg.342]    [Pg.182]    [Pg.79]    [Pg.186]    [Pg.273]    [Pg.191]    [Pg.128]    [Pg.260]    [Pg.6288]    [Pg.1743]    [Pg.403]   
See also in sourсe #XX -- [ Pg.22 , Pg.32 , Pg.33 ]




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A-Trypsin

Activated Hageman factor trypsin

Active centers trypsin

Amaranth trypsin inhibitor

Amidase trypsin

Amide hydrolysis Trypsin

Amylase-trypsin-inhibitors

Anionic trypsin

Basic pancreatic trypsin inhibitor (BPTI

Benzamidine, trypsin inhibition

Benzamidines trypsin inhibition

Benzoyl-trypsin

Bovin trypsin

Bovine Pancreatic Trypsin Inhibitor

Bovine Pancreatic Trypsin Inhibitor (BPTI) Simulations

Bovine Pancreatic Trypsin Inhibitor BPTI)

Bovine pancreatic trypsin

Bovine pancreatic trypsin inhibitor (BPT

Bovine pancreatic trypsin inhibitor simulations

Bovine pancreatic trypsine inhibitor

Bovine pancreatic trypsine inhibitor folding

Bovine trypsin inhibitor mutants

Bowman-Birk protease barley rootlet dual function a-amylase/trypsin

Bowman-Birk soybean trypsin inhibitor, amino

Bowman-Birk trypsin inhibitor

Brazilian pink beans, trypsin

Cancer tumor-associated trypsin inhibitor and

Cathepsin D, trypsin

Cationic trypsin

Cells, tumor trypsinized

Cellular Trypsin

Cereal a amylase/trypsin inhibitor family

Cereal a amylase/trypsin inhibitor family homologue

Chymotrypsin trypsin and

Chymotrypsin, Trypsin, and Related Enzymes

Citraconyl-BSA by Trypsin

Cleavage by trypsin

Collagen trypsin attack

Colostrum, trypsin inhibitor

Composition trypsin inhibitors from

Conjugate trypsin-dextran

Cowpea trypsin inhibitor

Dextran trypsin

Effects on trypsin

Egg trypsin inhibitor inactivation

Egg white trypsin inhibitor

Eleusine coracana trypsin/"/-amylase inhibitor

Encapsulate trypsin

Enzyme Assays Trypsin Activity

Enzymes trypsin

Factor , trypsin

Films trypsin

Folding of bovine pancreatic trypsin

Glutaraldehyde immobilization trypsin

Great Northern bean, trypsin

Human pancreatic secretory trypsin

Human trypsin

Immunoreactive trypsin

In-gel trypsin digestion

Inhibition, trypsin digestion

Inhibitor of trypsin

Inhibitors, enzymes trypsin activity

Insulin trypsin inhibitors

Inter-a-trypsin inhibitor

Kallikrein-trypsin inhibitor - Aprotinin

Kunitz trypsin inhibitor

Kunitz-type soybean trypsin

Kunitz-type soybean trypsin inhibitors

Ligand trypsin

Lima bean trypsin inhibitor

Mustard trypsin

Mustard trypsin inhibitor

Mustard trypsin thrombin inhibitor

Mutation in trypsin

Native protein structures bovine pancreatic trypsin inhibitor

Naturally Occurring Trypsin Inhibitors

Onion trypsin

P-Trypsin

Pancreas trypsin inhibitors

Pancreatic enzymes trypsin

Pancreatic trypsin inhibitor

Pancreatic trypsin inhibitor system

Pancreatic trypsin inhibitor, molecular

Pancreatic trypsin inhibitor, molecular dynamics simulation

Pancreatic trypsin inhibitor, structure

Pancreatic tumors trypsin

Pancreatitis Trypsin

Pancreatitis cationic trypsin

Papain trypsin hydrolysis

Peptide trypsin-catalyzed

Plant Kunitz serine protease inhibitor effects on trypsin

Plant serpins effects on trypsin

Plasma trypsin inhibitor

Polypropylene trypsin

Porcine pancreatic trypsin

Potato type II serine protease inhibitor effects on trypsin

Proenzymes, trypsin

Protease inhibitors pancreatic trypsin inhibitor

Protease inhibitors trypsin

Protein Engineering of Trypsin-Like Proteases

Protein Fragmentation Trypsin

Proteins trypsin

Pumpkin fruit trypsin inhibitor

Radiation Trypsin

Serine proteases trypsin

Serine trypsin

Soy Bean Trypsin Inhibitor

Soy trypsin inhibitor

Soybean trypsin inhibitor

Soybean trypsin inhibitor (SBTI

Soybean trypsin inhibitor structure

Soybean trypsin inhibitor, enzymatic

Squash family serine protease inhibitor effects on trypsin

Squash trypsin inhibitors

Substrate specificity of trypsin

Swine trypsin

Three-dimensional structures trypsin

Triose phosphate isomerase trypsin

Trypsin

Trypsin

Trypsin 0.2 percent

Trypsin Activity

Trypsin Interferon

Trypsin X-ray crystal structure

Trypsin absorption spectrum

Trypsin activated

Trypsin activation

Trypsin activation energy

Trypsin activation volumes

Trypsin active serine, mechanism

Trypsin active site

Trypsin active site region

Trypsin activity enhancement

Trypsin alkaline phosphatase

Trypsin and

Trypsin and trypsinogen

Trypsin aqueous solution

Trypsin assay

Trypsin binding

Trypsin bovine

Trypsin catalytic activity

Trypsin catalytic triad

Trypsin catalyzed condensation

Trypsin catalyzed hydrolysis and

Trypsin characteristics

Trypsin chromatography

Trypsin chymotrypsins and

Trypsin complex

Trypsin composition

Trypsin condensation

Trypsin crystal

Trypsin deficiency

Trypsin denaturation

Trypsin determination

Trypsin difference spectra

Trypsin digest

Trypsin digestion

Trypsin dipoles

Trypsin distribution

Trypsin elastase and

Trypsin endogenous proteolytic enzymes

Trypsin engineering

Trypsin enzymatic hydrolysis

Trypsin ester hydrolysis

Trypsin family

Trypsin fibers

Trypsin homologous sequences

Trypsin hydrogen-bonding network, structur

Trypsin hydrolysis

Trypsin hydrolysis studies

Trypsin hydrolysis/HPLC/thermospray

Trypsin hydrolysis/HPLC/thermospray analysis

Trypsin immobilization

Trypsin inhibition

Trypsin inhibitor

Trypsin inhibitor (basic pancreatic

Trypsin inhibitor activity

Trypsin inhibitor homologue

Trypsin inhibitor pancreatic, molecular weight

Trypsin inhibitor protein

Trypsin inhibitor spectra

Trypsin inhibitor, residual

Trypsin inhibitor, solution preparation

Trypsin inhibitors actions/effects

Trypsin inhibitors domain structure

Trypsin inhibitors folding

Trypsin inhibitors legumes

Trypsin inhibitors molecular modeling

Trypsin inhibitors supplementation

Trypsin inhibitors vitamin

Trypsin insulin degradation

Trypsin mimic

Trypsin model

Trypsin mutation

Trypsin myosin fragmentation

Trypsin neurotoxin

Trypsin oxyanion hole, structure

Trypsin pancreatin

Trypsin peptides

Trypsin poly

Trypsin production

Trypsin production inhibition

Trypsin production inhibition by hederagenin

Trypsin proinsulin cleavage

Trypsin proteases

Trypsin protein digestion

Trypsin protein hydrolysis

Trypsin protein-derivatives hydrolysis

Trypsin proteolysis

Trypsin ribonuclease

Trypsin solubility

Trypsin solution behavior

Trypsin solution preparation

Trypsin specificity

Trypsin stock

Trypsin streptokinase

Trypsin structure

Trypsin substrate analog inhibitor

Trypsin substrate binding

Trypsin substrates

Trypsin titration

Trypsin titration curves

Trypsin transition temperature

Trypsin treatment

Trypsin treatment sensitivity

Trypsin trimethylethoxysilane

Trypsin trimethylsilanol

Trypsin turnover number

Trypsin with versene

Trypsin, III

Trypsin, action

Trypsin, activity during pancreas

Trypsin, applications

Trypsin, calcium binding

Trypsin, chymotrypsin, cathepsin

Trypsin, chymotrypsin, cathepsin protease inhibitors

Trypsin, hydrolysis catalyzed

Trypsin, immobilized

Trypsin, molecular surfaces

Trypsin, peptide cleavage with

Trypsin, protein digestion using

Trypsin, purification

Trypsin, reversed-phase chromatography

Trypsin, sequencing peptides with

Trypsin, therapeutic enzyme

Trypsin-benzamidine complex

Trypsin-containing cell suspension

Trypsin-like Proteinases

Trypsin-like activity

Trypsin-like immunoreactivity

Trypsin-like proteases

Trypsin-like serine protease factor

Trypsin-like serine protease, function

Trypsin-like subunit

Trypsin-link activity

Trypsin-modulating oostatic factor

Trypsin/a-amylase

Trypsination

Trypsination

Trypsine aminopeptidase

Trypsinization

Trypsinization

Trypsinization mouse embryo cells

Trypsinized proteins

Trypsinogen-Trypsin Transition

Trypsins, fish

Trypsins, pancreatic

Tumor-associated trypsin inhibitor

Xa, Xlla, kallikrein, plasmin, trypsin

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