Die Aminosäuresequenz des doppelköpfigen Proteinaseninhibitors aus der Glandula submandibularis des Hundes, II. Ein Methioninrest als reaktives Hemmzentrum für Chymotrypsin
- 1 January 1975
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 356 (2) , 1859-1864
- https://doi.org/10.1515/bchm2.1975.356.2.1859
Abstract
The canine submandibular inhibitor is double-headed with 2 independent reactive sites. Whereas the trypsin-reactive center (-Ala-Cys-Pro-Arg26-Leu-His-) is located in domain I, the chymotrypsin-reactive site (-Met-Cys-Thr-Met78-Asp-Tyr-) is located in domain II. The presence of a methionine residue in this inhibition center is supported by the findings that nitration with tetranitromethane abolishes neither trypsin nor chymotrypsin inhibition; after alkylation of the methione residues, only trypsin inhibition is retained. Another inhibitor from microbial sources which also contains a methionine residue in the presumed reactive site also inhibits subtilisin but not chymotrypsin (or trypsin).This publication has 4 references indexed in Scilit:
- The Amino Acid Sequence of the Double-Headed Proteinase Inhibitor from Canine Submandibular Glands, III. Sequencing studiesHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1975
- Biochemistry of Natural Proteinase InhibitorsAngewandte Chemie International Edition in English, 1974
- Tetranitromethane. A Reagent for the Nitration of Tyrosyl Residues in Proteins*Biochemistry, 1966
- Modification of the Methionine Residues in Ribonuclease*Biochemistry, 1962