Purification of a soluble phospholipase A2 from synovial fluid in rheumatoid arthritis.

Purification of a soluble phospholipase A2 from synovial fluid in rheumatoid arthritis.
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从类风湿关节炎滑液中纯化可溶性磷脂酶 A2。

DOI:
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发表时间:
1986
期刊:
Journal of Biochemistry (Tokyo)
影响因子:
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通讯作者:
P. Vadas
P. Vadas
中科院分区:
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文献类型:
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作者:
E. Stefanski;Waldemar Pruzanski;Berit Sternby;P. Vadas

文献摘要

被引文献

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从人类风湿滑液中纯化了一种可溶性磷脂酶A2(PLA2),纯化倍数为4500倍。制备的十二烷基硫酸钠聚丙烯酰胺凝胶电泳法显示PLA2有两条相对分子质量分别为15,000和17,000和p1 4.2-5.0的区带。纯化的磷脂酰胆碱具有绝对的2-酰基专一性,在pH 7.5~8.0范围内对磷脂酰胆碱有最高活性,在pH 7.0时对磷脂酰乙醇胺有最高活性。放射免疫分析表明,人滑液PLA2与抗人胰腺PLA2无交叉反应。
A soluble phospholipase A2 (PLA2) was purified 4,500-fold from human rheumatoid synovial fluid. Preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis yielded two bands of PLA2 activity of molecular weights 15,000 and 17,000 and pl 4.2-5.0. Purified PLA2 had absolute 2-acyl specificity, and hydrolyzed phosphatidylcholine with optimal activity at pH 7.5-8.0 and phosphatidylethanolamine with optimal activity at pH 7.0. Human synovial fluid PLA2 did not cross-react with anti-human pancreatic PLA2, as tested by radioimmunoassay.