[Comparative study of active site structure in bovine and Pacific salmon trypsins].
The kinetic investigation was carried out on the inhibition of hydrolysis of N, alpha-benzoyl-D, L-arginine-p-nitroanilide (BApNA) for bovine and salmon trypsin by phenylmethanesulphonyl fluoride (PMSF), N, alpha-tosyl-L-lysine chloromethyl ketone (N-TLCK), N, alpha-tosyl-L-phenylalanine chloromethyl ketone (N-TPCK). Kinetic parameters of inhibition (Ki, k2) by PMSF for salmon and bovine trypsin differ insignificantly. The k2/Ki value of N-TPCK for salmon trypsin is 10 times more than of bovine trypsin. Kinetic parameters of inhibition by N-TLCK had the less difference. The Ki value of this inhibitor for salmon trypsin is 5 times less than that of bovine trypsin and k2 value is 1.7 times less.
Taran
L D
LD
Samus
N V
NV
D000818:Animals; D001586:Benzoylarginine Nitroanilide / Q000378:metabolism; D001665:Binding Sites; D002384:Catalysis; D002417:Cattle / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D012474:Salmon / Q000378:metabolism*; D013045:Species Specificity; D014357:Trypsin / Q000737:chemistry*; D014361:Trypsin Inhibitors / Q000494:pharmacology
D014361:Trypsin Inhibitors; D001586:Benzoylarginine Nitroanilide; D014357:Trypsin
Sravnitel'noe issledovanie struktury aktivnykh tsentrov tripsina byka i tikhookeanskikh lososevykh.