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Trypsinized proteins

An interesting report by P an and Jegier noted an increase in serum trypsin protein esterase in association with pulmonaiy vascular lesions in rabbits chronically exposed to ozone at 0.4 ppm. This serum a,-macroglobulin, which is synthesized in the liver, has been reported to be increased in human vascular disorders, but its physiologic significance is unknown. [Pg.363]

P an, A. Y. S., and Z. Jegier. Trypsin protein esterase in relation to ozone-induced vascular damage. Arch. Environ. Health 24 233-236, 1972. [Pg.384]

Increased serum trypsin protein Rabbit esterase... [Pg.682]

Lanthanides are better cofactors than Ca2+ for the activation of trypsinogen by trypsin. Proteins like calmodulin retain their biochemical activity even after substitution by a lanthanide. This is due to the same degree of conformational changes produced by Ca2+ and Ln3+ ions. But most Ca2+ requiring proteins function less effectively on substitution... [Pg.861]

One method of sample preparation proposed for MS/MS analysis of proteins is by performing enzymatic hydrolysis of gel pieces from SDS-PAGE (see paragraph 7.3.1) using trypsin, proteins are hydrolyzed at the carboxyl side of lysine and arginine residues. Protocol of enzymatic digestion and sample preparation is reported in Table 7.8. [Pg.277]

Figure 8.1. Conserved positions are often of functional importance. Alignment of trypsin proteins of mouse (SWISS-PROT P07146) and crayfish (SWISS-PROT P00765). Identical residues are underlined. Indicated above the alignments are three disulfide bonds (—s-s—), with participating cysteine residues conserved, amino acids side chains involved in the charge relay system (asterisk), and active side residue governing substrate specificity (diamond). Figure 8.1. Conserved positions are often of functional importance. Alignment of trypsin proteins of mouse (SWISS-PROT P07146) and crayfish (SWISS-PROT P00765). Identical residues are underlined. Indicated above the alignments are three disulfide bonds (—s-s—), with participating cysteine residues conserved, amino acids side chains involved in the charge relay system (asterisk), and active side residue governing substrate specificity (diamond).
Trypsin Protein hydrolysis (for details see industrial section above) Inflammation Spectrophotometry or microcalorimetry One BAEE (Af-benzoyl-L-arginine ethyl ester) unit is an absorbance change at 253 nm of 0.001 per min with BAEE as substrate at pH 7.6 and 25°C... [Pg.1146]

Figure 5.5 Early MALDI mass spectra obtained using solid nicotinic acid (3-carboxyl pyridine) as matrix and a Q-switched frequency-quadrupled Nd YAG laser (266 nm, 10 ns). Mass spectrum of porcine trypsin (protein of molecular mass 23 463 Da) (a) full range spectrum (b) expanded region showing protein peaks. Reproduced from Karas and Hillenkamp, Anal Chem. 60, 2299 (1988), copyright (1988), with permission of the American Chemical Society. Figure 5.5 Early MALDI mass spectra obtained using solid nicotinic acid (3-carboxyl pyridine) as matrix and a Q-switched frequency-quadrupled Nd YAG laser (266 nm, 10 ns). Mass spectrum of porcine trypsin (protein of molecular mass 23 463 Da) (a) full range spectrum (b) expanded region showing protein peaks. Reproduced from Karas and Hillenkamp, Anal Chem. 60, 2299 (1988), copyright (1988), with permission of the American Chemical Society.
Dilute each sample with water so as to obtain a urea concentration of less than 1 M, and digest with trypsin (at a weight/ weight ratio of 1 25 for Trypsin-protein) overnight at 37 °C. [Pg.120]

The term catalysis was applied to the biological phenomena listed above and to several other reactions discovered in the next several years. The active component of bitter almonds was named emulsin in 1837. Other carbohydrate-splitting activities (ptyalin in saliva, amylase in malt) had already been described. Pepsin and trypsin, protein-digesting agents from the stomach and pancreas, were also discovered during this period. The activities of these materials were contrasted with the materials responsible for fermentation. Early theories of Willis and of Stahl to explain fermentation as a disruption caused by violent motion of... [Pg.1]

Carboaypeptidases tpre-carboxypeptidesel Trypsin Proteins and polypeptides Cleavis terminal ammo acids... [Pg.283]


See other pages where Trypsinized proteins is mentioned: [Pg.260]    [Pg.362]    [Pg.371]    [Pg.3]    [Pg.574]    [Pg.96]    [Pg.110]    [Pg.405]    [Pg.115]    [Pg.442]    [Pg.188]    [Pg.3048]    [Pg.729]    [Pg.1872]    [Pg.44]   
See also in sourсe #XX -- [ Pg.110 ]




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Native protein structures bovine pancreatic trypsin inhibitor

Protein Engineering of Trypsin-Like Proteases

Protein Fragmentation Trypsin

Proteins trypsin

Proteins trypsin

Trypsin

Trypsin inhibitor protein

Trypsin protein digestion

Trypsin protein hydrolysis

Trypsin protein-derivatives hydrolysis

Trypsin trypsinization

Trypsin, protein digestion using

Trypsination

Trypsinization

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