[Some physicochemical properties of modified trypsin].
Physico-chemical properties of trypsin covalently bound with human serum albumin by glutaric aldehyde have been studied. The modification of the enzyme practically caused no changes in the pH optimum of trypsin. The inhibition of modified trypsin by inhibitors from soy beans and human blood serum has been also studied. The apparent inhibition constants have been calculated. The modification has been shown to result in a deceleration of autolytic degradation. The autolysis rate constants have been calculated at 50 degrees C.
D055598:Chemical Phenomena; D002621:Chemistry; D005976:Glutaral; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011485:Protein Binding; D012709:Serum Albumin; D013025:Glycine max; D013329:Structure-Activity Relationship; D014357:Trypsin / Q000378:metabolism*; D014361:Trypsin Inhibitors / Q000097:blood / Q000494:pharmacology
D012709:Serum Albumin; D014361:Trypsin Inhibitors; D014357:Trypsin; D005976:Glutaral
Nekotorye fiziko-khimicheskie svoĭstva modifitsirovannogo tripsina