Limited Proteolysis of Glucose Dehydrogenase fromBacillus megateriumby Proteinase K
- 1 January 1983
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 364 (2), 839-844
- https://doi.org/10.1515/bchm2.1983.364.2.839
Abstract
Glucose dehydrogenase from B. megaterium is subjected to proteolysis with proteinase K. Upon proteolysis the enzyme is inactivated and the polypeptide chain is cleaved into 2 distinct fragments. These components designated as K-protein and K-peptide have MW of 26,000 and 3000 [daltons], respectively. Under native conditions the K-protein and K-peptide remain associated and the tetrameric structure of the proteolytically modified enzyme is preserved. The K-protein and K-peptide were isolated and characterized. The cleavage occurs in the C-terminal region of the polypeptide chain. -Leu Ala .dwnarw. Ser-Ser-Glu is proposed as the cleavage site.This publication has 7 references indexed in Scilit:
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