猪粒细胞中两种低分子量钙结合蛋白的分离及N端序列分析

Isolation and N-terminal sequence of two low molecular weight calcium-binding proteins from pig granulocytes.

Schleicher C H, Dell'Angelica E C, Santomé J A

Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Argentina.

Int J Biochem. 1993 Sep;25(9):1251-6. doi: 10.1016/0020-711x(93)90075-p.

Abstract

Two small, abundant calcium-binding proteins were isolated from pig granulocytes. They were named p7A and p7B. Relative molecular masses were approx. 32,000 for p7A and 13,000 for p7B, when obtained by Sephadex G-75 gel filtration, while it was 7000 for both proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). 2. N-terminal sequence analysis suggests that p7A is homologous to human and mouse MRP-8 and that p7B may be related to human and mouse MRP-14, though some properties of the latter--such as mobility on SDS-PAGE--were found to be different. In addition, p7A and p7B could be resolved under native conditions, contrasting with the fact that human and mouse MRP-8/MRP-14 form noncovalent complexes.

摘要

从猪粒细胞中分离出两种小的、含量丰富的钙结合蛋白。它们被命名为p7A和p7B。通过葡聚糖G-75凝胶过滤法测得，p7A的相对分子质量约为32000，p7B为13000；而通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）测得，两种蛋白的相对分子质量均为7000。2. N端序列分析表明，p7A与人及小鼠的MRP-8同源，p7B可能与人及小鼠的MRP-14相关，不过发现后者的一些特性，如在SDS-PAGE上的迁移率，有所不同。此外，p7A和p7B在天然条件下可以分离，这与人及小鼠的MRP-8/MRP-14形成非共价复合物的情况不同。