THE PRIMARY STRUCTURE OF A MEMBRANE-ASSOCIATED PHOSPHOLIPASE-A2 FROM HUMAN SPLEEN
THE PRIMARY STRUCTURE OF A MEMBRANE-ASSOCIATED PHOSPHOLIPASE-A2 FROM HUMAN SPLEEN
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DOI：
10.1016/0006-291x(89)92096-2
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发表时间：
1989-08-30
影响因子：
3.1
通讯作者：
OKAMOTO, M
中科院分区：
文献类型：
--
作者：
KANDA, A;ONO, T;OKAMOTO, M
通过对赖氨酰内肽酶和金黄色葡萄球菌 V8 蛋白酶切割产生的肽进行序列分析，确定从人脾膜组分中纯化的膜相关磷脂酶 A2 的完整一级结构。该酶由 124 个氨基酸残基组成，对应的分子量为 13,904。一级结构揭示了II类磷脂酶A2的特征，并且碱性氨基酸残基与酸性氨基酸残基的比例很大，该比例为3.4:1。
The complete primary structure of membrane-associated phospholipase A2 purified from a human splenic membrane fraction was determined by sequence analysis of the peptides generated by lysyl endopeptidase and Staphylococcus aureus V8 protease cleavage. The enzyme consists of 124 amino acid residues corresponding to a molecular weight of 13,904. The primary structure reveals the characteristics of Group II phospholipases A2 and a large ratio of basic amino acid residues to acidic ones, that ratio being 3.4:1.