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  • Title: Similarity in active site arrangement of neutral protease from calf thymus chromatin and trypsin.
    Author: Kowalska-Loth B, Zieleński J, Toczko K, Chmielewska I.
    Journal: Acta Biochim Pol; 1976; 23(2-3):139-44. PubMed ID: 987680.
    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.
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