[Interaction of trypsin with a trypsin inhibitor from bovine colostrum].
Kinetics of trypsin association with trypsin inhibitor from colostrum (IC) was studied. The association rate constant is 3-10-5 M- minus 1 sec- minus 1 at pH 7,8, 25 degrees C. The rate constant for the complex dissociation was determined from the kinetics of the IC displacement from the complex with trypsin by a specific substrate and was found to be 5-10- minus 6 sec- minus 1 (pH 7,8; 25 degrees C). The equilibrium constant (Ki) was measured in a special experiment and was equal to 4-10- minus 12 M (p H 7,8; 25 degrees C). The similarity of this reaction and the association of trypsin with other protein inhibitors was discussed.
D000818:Animals; D001120:Arginine / Q000378:metabolism; D001565:Benzoates / Q000378:metabolism; D002417:Cattle; D003126:Colostrum / Q000201:enzymology*; D004347:Drug Interactions; D004950:Esterases / Q000378:metabolism; D005260:Female; D006868:Hydrolysis; D007700:Kinetics; D014357:Trypsin / Q000378:metabolism / Q000494:pharmacology*; D014361:Trypsin Inhibitors / Q000378:metabolism / Q000494:pharmacology*
D001565:Benzoates; D014361:Trypsin Inhibitors; D001120:Arginine; D004950:Esterases; D014357:Trypsin
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