title: Similarity in active site arrangement of neutral protease from calf thymus chromatin and trypsin.
abstract: 1. Susceptibility to inhibitors of neutral protease from calf thymus chromatin has been compared with that of trypsin. The chromatin protease reacts stoichiometrically with the inhibitors specific for trypsin (diisopropylfluorophosphate, tosyl-lysyl chloromethane, soybean trypsin inhibitor and Kunitz basic inhibitor from pancreas), but not with the inhibitor specific for chymotrypsin (tosyl-phenylalanyl chloromethane). 2. Chromatin protease, similarly as trypsin, cleaves Lys-X and Arg-X peptide bonds. 3. It is concluded that the structure of active site region of both enzymes is very similar.
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002843:Chromatin / Q000201:enzymology*; D006657:Histones / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors; D011485:Protein Binding; D013329:Structure-Activity Relationship; D013950:Thymus Gland / Q000201:enzymology*; D014357:Trypsin / Q000378:metabolism*; D014361:Trypsin Inhibitors / Q000494:pharmacology
chemical_list: D002843:Chromatin; D006657:Histones; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D010447:Peptide Hydrolases; D014357:Trypsin