Effects of platinum complexes on chymotrypsin.
A variety of platinum complexes were evaluated as inhibitors of alpha-chymotrypsin. A standard enzyme assay was used with benzoyl-L-tyrosine ethyl ester as the substrate. Rb2PtBr4, trans-Pt(NH3)2Cl2, and K2PtCl4 were all effective enzyme inhibitors. Pt(Gly-L-Met(Cl2, Pt(Met)(NH3)2Cl, cis-Pt(NH3)2Cl2, and two ethylenediamminedichloroplatinum complexes were weak inhibitors of alpha-chymotrypsin. A surprising finding was the noninhibition of an immobilized preparation of alpha-chymotrypsin by the above inhibitors and by active-site-directed modifying reagents.
D000818:Animals; D000970:Antineoplastic Agents / Q000494:pharmacology*; D002417:Cattle; D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D002945:Cisplatin / Q000031:analogs & derivatives / Q000494:pharmacology; D004800:Enzymes, Immobilized / Q000037:antagonists & inhibitors; D066298:In Vitro Techniques; D010984:Platinum / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D000970:Antineoplastic Agents; D004800:Enzymes, Immobilized; D010984:Platinum; D002918:Chymotrypsin; D002945:Cisplatin