A phosphatidylinositol-specific phospholipase C was purified from the culture broth of Bacillus thuringiensis IAM 12077 to a homogeneous state as revealed by polyacrylamide gel electrophoresis. The specific activity of the purified enzyme was 559 units/mg and recovery of the enzyme activity was 31%. Molecular and physiological properties of the purified enzyme, including molecular weight (22,000), isoelectric point (pI = 4.9) and its ectoenzyme-releasing activity, were studied in comparison with those other known enzymes of bacterial origin.
Complete purification of phosphatidylinositol-specific phospholipase C from a strain of Bacillus thuringiensis. Publishing Authors By Initials
Complete purification of phosphatidylinositol-specific phospholipase C from a strain of Bacillus thuringiensis. Journal Published:
PUBLICATION TYPE: Research Support, Non-U.S. Gov
Journal: Journal of biochemistry
VOLUME: 93
Page Numbers: 1717-9
Journal Abbreviation: J. Biochem.
ISSN: 0021-924X
DAY: 19
MONTH: Jun
YEAR: 1983
Complete purification of phosphatidylinositol-specific phospholipase C from a strain of Bacillus thuringiensis. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 376600
Complete purification of phosphatidylinositol-specific phospholipase C from a strain of Bacillus thuringiensis. Keywords Mesh Terms:
KEYWORDS: Type C Phospholipases
MESH TERMS: isolation & purification
Chemical & Substance for Abstract: Complete purification of phosphatidylinositol-specific phospholipase C from a strain of Bacillus thuringiensis. Information
Substance Name: Type C Phospholipases
Registry Number: EC 3.1.4.-
Grant and Affiliation Information for Complete purification of phosphatidylinositol-specific phospholipase C from a strain of Bacillus thuringiensis.
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Country: JAPAN
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MEDLINETA: J Biochem
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