α-糜蛋白酶 来源于牛胰腺(纯化)

α-胰凝乳蛋白酶

N-Succinyl-Gly-Gly-Phe-p-nitroanilide, protease substrate | Chymotrypsin Substrate I, Colorimetric | N-(3-Carboxy-1-oxopropyl)glycylglycyl-N-(4-nitrophenyl)-L-phenylalaninamide | AKOS024350585 | 4-[[2-[[2-[[1-(4-nitroanilino)-1-oxo-3-phenylpropan-2-yl]ami

C129080-100mg

100mg

EnzymoPure™

≥45 units/mg protein

Chymotrypsin preferentially catalyzes the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine and tryptophan. It also readily acts upon amides and esters of susceptible amino acids. Chymotrypsin catalyzes the hydrolysis of bonds of leucyl, methionyl, asparaginyl and glutamyl residues. Chymotrypsin preferentially catalyzes the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine and tryptophan. It also readily acts upon amides and esters of susceptible amino acids. Chymotrypsin catalyzes the hydrolysis of bonds of leucyl, methionyl, asparaginyl and glutamyl residues.

一种丝氨酸蛋白酶，能将与芳香烃或其他大型疏水性侧链（Tyr、Trp、Phe、Met、Leu）结合的肽从键的羧基端水解。 α-Chymotrypsin is a serine peptidase and has 241 amino acid residues contained in three polypeptide chains (A chain-13 residues, B chain-131 residues, and C chain-97 residues) linked by disulfide bridges. Molecular weight of this enzyme is found to be 25 kDa. Its pI is 8.75. It selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine. Ca2+ activates and stabilizes the enzyme. The enzyme is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), chymostatin, aprotinin, α1-antitrypsin, and α2-macroglobulin, 10 mM Cu2+ and Hg2+.