Extracellular phospholipase A2 was purified about 1.7 X 10(5) fold to near homogeneity from human synovial fluid of rheumatoid arthritis by sequential use of column chromatographies on heparin-Sepharose, butyl-Toyopearl, and reversed-phase HPLC. The final preparation showed a single band on SDS-polyacrylamide gel electrophoresis, and its molecular mass was estimated to be approximately 13,700 daltons. The purified enzyme had a pH optimum of 9.0 and required Ca2+ for maximum activity. It hydrolyzed phosphatidyl-ethanolamine more effectively than phosphatidylserine and phosphatidylcholine. These properties were similar to those of an extracellular phospholipase A2 detected in the peritoneal cavity of caseinate-treated rats.
Purification and characterization of extracellular phospholipase A2 from human synovial fluid in rheumatoid arthritis. Publishing Authors By Initials
Purification and characterization of extracellular phospholipase A2 from human synovial fluid in rheumatoid arthritis. Journal Published:
PUBLICATION TYPE: Research Support, Non-U.S. Gov
Journal: Journal of biochemistry
VOLUME: 105
Page Numbers: 395-9
Journal Abbreviation: J. Biochem.
ISSN: 0021-924X
DAY: 19
MONTH: Mar
YEAR: 1989
Purification and characterization of extracellular phospholipase A2 from human synovial fluid in rheumatoid arthritis. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 376600
Purification and characterization of extracellular phospholipase A2 from human synovial fluid in rheumatoid arthritis. Keywords Mesh Terms:
KEYWORDS: Synovial Fluid
MESH TERMS: enzymology
Chemical & Substance for Abstract: Purification and characterization of extracellular phospholipase A2 from human synovial fluid in rheumatoid arthritis. Information
Substance Name: Phospholipases A2
Registry Number: EC 3.1.1.4
Grant and Affiliation Information for Purification and characterization of extracellular phospholipase A2 from human synovial fluid in rheumatoid arthritis.
AFFILIATION: Department of Health Chemistry, Faculty of Pharmaceutical Sciences, University of Tokyo.
Country: JAPAN
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MEDLINETA: J Biochem
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