[Microcolorimetric study of the association of trypsin with a pancreatic inhibitor].
Enthalpy of the association of trypsin with pancreatic inhibitor from bovine pancreas at 25 degrees C as a function of pH and ionic strength is estimated. The dependence of the enthalpy on pH is of an extremal character with a minimum at pH 7.6 (delta H degrees =-10.3 ccal/mole). The increase of ionic strength with the addition of LiCl, KCl and CsCl at pH 7.6 leads to be increase of delta H degrees. Possible mechanisms of enthlpy changes depending on medium conditions are considered.
D000818:Animals; D002417:Cattle; D002586:Cesium; D055598:Chemical Phenomena; D002621:Chemistry; D003124:Colorimetry; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008094:Lithium; D009994:Osmolar Concentration; D010179:Pancreas / Q000378:metabolism*; D011189:Potassium Chloride; D013816:Thermodynamics; D014357:Trypsin; D014361:Trypsin Inhibitors
D014361:Trypsin Inhibitors; D002586:Cesium; D011189:Potassium Chloride; D008094:Lithium; D014357:Trypsin
Mikrokalorimetricheskoe izuchenie assotsiatsii tripsina a pankreaticheskim ingibitorom