Purification and characterization of membrane-bound phospholipase A2 from rat platelets.
Purification and characterization of membrane-bound phospholipase A2 from rat platelets.
复制标题
大鼠血小板膜结合磷脂酶 A2 的纯化和表征。
DOI：
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发表时间：
1988
期刊：
影响因子：
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通讯作者：
Keizo Inoue
中科院分区：
文献类型：
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作者：
Makio Hayakawa;Ichiro Kudo;Motowo Tomita;Keizo Inoue
磷脂酶A2从大鼠血小板膜溶解的1 M KCl和纯化的十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和HPLC接近均匀。将纯化的膜结合酶的特性与从凝血酶刺激的大鼠血小板释放的磷脂酶A2的特性进行比较（Horigome，K.，Hayakawa，M.，井上，K.，& Nojima，S.（1987）J.Biochem.101，625-631）。两种酶的分子量、反相HPLC洗脱曲线和NH 2-末端序列相同。这两种酶的其他特性，如比活性、底物特异性、最适pH、Ca 2+需求、热不稳定性和对溴苯甲酰甲基溴的敏感性也是不可区分的。这些发现表明这两种酶具有共同的结构。
Phospholipase A2 was solubilized from rat platelet membrane by 1 M KCl and purified to near homogeneity on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and HPLC. The characteristics of the purified membrane-bound enzyme were compared with those of phospholipase A2 released from thrombin-stimulated rat platelets (Horigome, K., Hayakawa, M., Inoue, K., & Nojima, S. (1987) J. Biochem. 101, 625-631). The molecular weights, elution profiles on reversed-phase HPLC, and NH2-terminal sequences were identical for the two enzymes. Other characteristics of the two enzymes, such as specific activity, substrate specificity, pH optimum, Ca2+ requirement, heat lability, and sensitivity to p-bromophenacyl bromide were also indistinguishable. These findings suggest that both enzymes share a common structure.