Similarity in active site arrangement of neutral protease from calf thymus chromatin and trypsin
Kowalska-Loth, B.; Zieleński, J.; Toczko, K.; Chmielewska, I.
Acta Biochimica Polonica 23(2-3): 139-144
1976
ISSN/ISBN: 0001-527X PMID: 987680 Document Number: 102036
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.