兔肝脏胞质溶胶中蛋白质Z的纯化与特性分析

Purification and characterization of protein Z from rabbit liver cytosol.

作者信息

Vincent S H, Holeman B, Muller-Eberhard U

出版信息

Biochem Biophys Res Commun. 1985 Oct 30;132(2):575-81. doi: 10.1016/0006-291x(85)91172-6.

Abstract

Protein Z was purified from rabbit liver cytosol by affinity chromatography on oleic acid-agarose and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis. After removal of sodium dodecyl sulfate, the renatured protein was found to bind heme and bilirubin with a Kd of approximately 1 microM which produced large red shifts in their absorption spectra. On isoelectric focusing, rabbit protein Z exhibited two main bands with pI around 6.0.

摘要

通过在油酸 - 琼脂糖上进行亲和色谱和制备性十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳，从兔肝胞质溶胶中纯化出蛋白质Z。去除十二烷基硫酸钠后，发现复性后的蛋白质能与血红素和胆红素结合，解离常数（Kd）约为1微摩尔，这使其吸收光谱产生了较大的红移。在等电聚焦时，兔蛋白质Z呈现出两条主要条带，其等电点（pI）约为6.0。