Similarity in active site arrangement of neutral protease from calf thymus chromatin and trypsin.
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.
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
D002843:Chromatin; D006657:Histones; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D010447:Peptide Hydrolases; D014357:Trypsin