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Trypsinization

As examples of applications, we present the overall accuracy of predicted ionization constants for about 50 groups in 4 proteins, changes in the average charge of bovine pancreatic trypsin inhibitor at pH 7 along a molecular dynamics trajectory, and finally, we discuss some preliminary results obtained for protein kinases and protein phosphatases. [Pg.176]

The presented algorithm was applied to 4 proteins (lysozyme, ribonuclease A, ovomucid and bovine pancreatic trypsin inhibitor) containing 51 titratable residues with experimentally known pKaS [32, 33]. Fig. 2 shows the correlation between the experimental and calculated pKaS. The linear correlation coefficient is r = 0.952 the slope of the line is A = 1.028 and the intercept is B = -0.104. This shows that the overall agreement between the experimental and predicted pKaS is good. [Pg.188]

M. H. Hao, M. R. Pincus, S. Rackovsky, and H. A. Scheraga. Unfolding and refolding of the native structure of bovine pancreatic trypsin inhibitor studied by computer simulations. Biochemistry, 32 9614-9631, 1993. [Pg.259]

In periodic boimdary conditions, one possible way to avoid truncation of electrostatic interaction is to apply the so-called Particle Mesh Ewald (PME) method, which follows the Ewald summation method of calculating the electrostatic energy for a number of charges [27]. It was first devised by Ewald in 1921 to study the energetics of ionic crystals [28]. PME has been widely used for highly polar or charged systems. York and Darden applied the PME method already in 1994 to simulate a crystal of the bovine pancreatic trypsin inhibitor (BPTI) by molecular dynamics [29]. [Pg.369]

Application of the CCM to small sets (n < 6) of enzyme inhibitors revealed correlations between the inhibitory activity and the chirality measure of the inhibitors, calculated by Eq. (26) for the entire structure or for the substructure that interacts with the enzyme (pharmacophore) [41], This was done for arylammonium inhibitors of trypsin, Di-dopamine receptor inhibitors, and organophosphate inhibitors of trypsin, acetylcholine esterase, and butyrylcholine esterase. Because the CCM values are equal for opposite enantiomers, the method had to be applied separately to the two families of enantiomers (R- and S-enantiomers). [Pg.419]

Brooks B and M Karplus 1983. Harmonic Dynamics of Proteins Normal Modes and Fluctuations in Bovine Pancreatic Trypsin Inhibitor. Proceedings of the National Academy of Sciences USA 80 6571-6575. [Pg.315]

Trypsin IVHPSYN.SN TLNNDIMLIK LKSAASLNSR VASISLP.. . TSCA..SAGT... [Pg.539]

Trypsin QCLISGWGN.TKSSGT SYPDVLKCLK APILSDSSCK SAYPGQITSN... [Pg.539]

Trypsin MFCAGYLEGG. . . KDSCQGD SGGPW..CS GK LQGI VSWGSGCAQK... [Pg.539]

Fig. 10.12 Sequence alignment of trypsin, chymotrypsin and thrombin (bovine). The active sites histidine, aspartic acid and serine are highlighted. Fig. 10.12 Sequence alignment of trypsin, chymotrypsin and thrombin (bovine). The active sites histidine, aspartic acid and serine are highlighted.
D, J Sturzebecher and WBode 1991. Geometry of Binding of the N-Alpha-Tosylated Piperidides of weffl-Amidino-Phenylalanine, Para Amidino-Phenylalanine and para-Guanidino-Phenylalanine to Thrombin and Trypsin - X-ray Crystal Structures of Their Trypsin Complexes and Modeling of their Thrombin Complexes. FEBS Letters 287 133-138. [Pg.578]

Guo Z and C L Brooks III 1998. Rapid Screening of Binding Affinities Application of the A-Dynamics Method to a Trypsin-Inhibitor System. Journal of the American Chemical Society 120 1920-1921. [Pg.651]

The so-called "trypsin," obtainable from pancreatic juice and from fresh extracts of the pancreas, is not a simple enzyme but a mixture of trypsin proper (which hydrolyses proteins to proteoses and peptones) and a series of enzymes which hydrolyse these breakdown products to their constituent amino-acids. The term trypsin," when used below, refers to this mixture. [Pg.517]

Since trypsin is a mixture, it has no well-defined optimum pH. It should also be noted that trypsin is the only hydrolytic enzyme which is at all active in alkaline solution. [Pg.517]

To the remainder of the casein solution add 0 5 to o 8 g. of finely powdered commercial trypsin, shake to dissolve, and place in a thermostat (or in an incubator) at 40 . After 15 minutes, remove 25 ml. and add a few drops of phenolphthalein it will now be found that the solution remains colourless. Run in carefully Mj 10 NaOH solution until the colour of the solution is just pink, add 5 ml, of neutralised formalin and then titrate against Mj 10 NaOH solution until the pink colour is just restored note the amount required. Remove fiirther quantities (rf 25 ml. at intervals which must be determined by the speed of the reaction. The following will probably make a suitable series i, 2, 3,... [Pg.518]

To the remainder of the gelatin solution, add 0 5 to o 8 g. of finely powdered commercial trypsin and incubate at 40 . Carry out the formaldehyde titration on 25 ml. samples at intervals as above. [Pg.519]

Urease is one of the enzymes which have been obtained in the crystalline state. This has been done by stirring jack bean meal with 30°o aqueous acetone, filtering and allowing the filtrate to remain at o for several hours. The urease which crystallises out is separated by centrifuging and is then recrystallised. Like crystalline pepsin and trypsin, it is a protein. [Pg.519]

The peptide shown m green was isolated by trypsin catalyzed hydrolysis and has an ammo acid sequence that completes the remaining overlaps... [Pg.1132]

Trypsin (Section 27 10) A digestive enzyme that catalyzes the hydrolysis of proteins Trypsin selectively catalyzes the cleavage of the peptide bond between the carboxyl group of lysine or arginine and some other amino acid... [Pg.1296]


See other pages where Trypsinization is mentioned: [Pg.66]    [Pg.99]    [Pg.157]    [Pg.230]    [Pg.299]    [Pg.408]    [Pg.2821]    [Pg.92]    [Pg.177]    [Pg.189]    [Pg.240]    [Pg.20]    [Pg.316]    [Pg.353]    [Pg.538]    [Pg.538]    [Pg.539]    [Pg.602]    [Pg.603]    [Pg.623]    [Pg.652]    [Pg.517]    [Pg.1130]    [Pg.1133]    [Pg.898]   
See also in sourсe #XX -- [ Pg.251 ]

See also in sourсe #XX -- [ Pg.54 ]

See also in sourсe #XX -- [ Pg.248 ]




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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 trypsinization

Trypsin trypsinization

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 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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