Chymotrypsin C
نویسندگان
چکیده
منابع مشابه
Chymotrypsin C (caldecrin) stimulates autoactivation of human cationic trypsinogen.
Trypsin-mediated trypsinogen activation (autoactivation) facilitates digestive zymogen activation in the duodenum but may precipitate pancreatitis if it occurs prematurely in the pancreas. Autoactivation of human cationic trypsinogen is inhibited by a repulsive electrostatic interaction between the unique Asp218 on the surface of cationic trypsin and the conserved tetra-aspartate (Asp19-22) mot...
متن کاملKinetics of the interaction of chymotrypsin with eglin c.
The kinetics of binding of recombinant eglin c to bovine pancreatic chymotrypsin was studied by conventional and stopped-flow techniques. With nanomolar enzyme and inhibitor concentrations, the inhibition was fast and pseudo-irreversible (k(assoc.) = 4 x 10(6) m-1.s-1 at 7.4 and 25 degrees C). Reaction of the enzyme-inhibitor complex with alpha 1-proteinase inhibitor, an irreversible chymotryps...
متن کاملAnalogues of acetyl chymotrypsin.
Previous papers (1, 2) have reported the acylation of chymotrypsin with several nitrophenyl acetates. It was of obvious interest to test the behavior of nitrophenyl esters of other acids in the same connection. It now appears that chymotrypsin may be acylated by a number of acids differing considerably from acetic acid in structure. Beneoyl and salicyl chymotrypsins were prepared and found to r...
متن کاملSpecificity of chymotrypsin B.
Brown, Shupe, and Laskowski (1) have described the isolation, from beef pancreas, of a crystalline proteolytic enzyme which they have named “activated protein B” or “chymotrypsin B.” Through the kindness of Dr. Laskowski who provided us with a 4 times recrystallized sample of this enzyme, it was possible to examine its action on a series of synthetic peptides and peptide derivatives. The data p...
متن کاملPurification, cDNA cloning, and recombinant expression of chymotrypsin C from porcine pancreas.
Chymotrypsin C is a bifunctional secretory-type serine protease in pancreas; besides proteolytical activity, it also exhibits a calcium-decreasing activity in serum. In this study, we purified activated chymotrypsin C from porcine pancreas, and identified its three active forms. Active chymotrypsin C was found to be different in the length of its 13-residue activation peptide due to carboxydipe...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1965
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)97634-9