leupeptins and benzoylarginine-ethyl-ester

leupeptins has been researched along with benzoylarginine-ethyl-ester* in 1 studies

Other Studies

1 other study(ies) available for leupeptins and benzoylarginine-ethyl-ester

ArticleYear
Kinetic and structural properties of two isoforms of trypsin isolated from the viscera of Japanese anchovy, Engraulis japonicus.
    Journal of protein chemistry, 2001, Volume: 20, Issue:1

    Two isoforms of anchovy trypsin (aT-I and aT-II) were purified from the visceral extracts by (NH4)2SO4 fractionation followed by affinity chromatography, gel filtration, and ion-exchange chromatography. The homogeneity of the purified preparation was evidenced by both native- and SDS-PAGE, and further by gelatin zymography. Identities of aT-I and aT-II as trypsins were established by N-terminal amino acid sequencing, which matched exactly to the corresponding stretches of their respective amino acid sequences obtained by molecular cloning [Ahsan et al. (2000), Marine Biotechnol., in press]. Both isoforms were completely inhibited by serine protease inhibitors as well as by specific trypsin inhibitors. The purified anchovy trypsins showed considerably higher catalytic efficiencies (kcat/Km) than bovine trypsin as measured toward benzoyl-arginine p-nitroanilide (BAPA) and benzoyl-arginine ethyl ester (BAEE) at 25 degrees C; in particular, aT-II was 35 times more efficient than its mammalian counterpart against BAPA. This was due mainly to a dramatic decrease of Km values for anchovy trypsins, which are indicative of an evolutionary response toward increased substrate binding at suboptimal temperatures in the marine environment.

    Topics: Amino Acid Sequence; Animals; Antipain; Arginine; Benzoylarginine Nitroanilide; Enzyme Stability; Fishes; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Leupeptins; Molecular Sequence Data; Molecular Weight; Trypsin; Trypsin Inhibitors; Viscera

2001
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