Purification and N-terminal sequence analysis of Streptomyces chromofuscus phospholipase D.
Purification and N-terminal sequence analysis of Streptomyces chromofuscus phospholipase D.
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色褐链霉菌磷脂酶 D 的纯化和 N 端序列分析。
DOI：
10.1159/000236934
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发表时间：
1995
影响因子：
2.8
通讯作者：
Kennerly,DA
中科院分区：
文献类型：
--
作者：
Dinh,TT;McClure,GD;Kennerly,DA
用染料亲和层析和非变性聚丙烯酰胺凝胶电泳（PAGE）对部分纯化的商业磷脂酶D（PLD）进行了分级。活性物质在SDS-PAGE上迁移为三条带。两个丰度较高的物种显示具有相同的N-末端序列，而第三条带的数量要少得多，并且具有不同的序列。克隆显色褐链霉菌PLD将允许构建允许PLD调控表达的肥大细胞系的稳定转染子。
Partially purified commercial phospholipase D (PLD) was fractionated by dyeligand affinity chromatography and nondenaturing polyacrylamide gel electrophoresis (PAGE). Active material migrated as three bands on SDS-PAGE. The two higher-abundance species were shown to have identical N-terminal sequences, while the third band was present in much smaller amounts and had a distinct sequence. CloningStreptomyces chromofuscusPLD will allow the construction of stable transfectants of mast cell lines permitting regulated expression of PLD.