Membrane-bound and soluble extracellular alpha-amylase from Bacillus subtilis.
作者： P. Mäntsälä , H. Zalkin
DOI: 10.1016/S0021-9258(19)86926-0
关键词:
摘要: Extracellular alpha-amylase was purified to homogeneity from a Marburg strain of Bacillus subtilis. The enzyme is single polypeptide chain molecular weight approximately 67,000. Its NH2-terminal amino acid sequence Leu-Thr-Ala-Pro-Ser-Ile-Lys. A membrane-derived solubilizing membrane vesicles by treatment with Triton X-100 and highly chromatography on an anti-alpha-amylase-protein A-Sepharose column. Membrane-derived indistinguishable the soluble extracellular sodium dodecyl sulfate-gel electrophoresis radioimmunoassay. contains phospholipid. Approximately 30 80% phospholipid extracted chloroform:methanol. predominately phosphatidylethanolamine. Treatment phospholipase D released phosphatidic acid. Membrane-bound latent in vesicles. Release membrane-bound endogenous maximal at pH 8.5, inhibited metal chelators diisopropyl fluorophosphate stimulated Ca2+ Mg2+. amount related level secretion.
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