PURIFICATION AND CRYSTALLIZATION OF 15-LIPOXYGENASE FROM RABBIT RETICULOCYTES

被引：28

作者：

SLOANE, DL

BROWNER, MF

DAUTER, Z

WILSON, K

FLETTERICK, RJ

SIGAL, E

机构：

[1] UNIV CALIF SAN FRANCISCO,CARDIOVASC RES INST,PROGRAM EXCELLENCE MOLEC BIOL,BOX 0911,SAN FRANCISCO,CA 94143

[2] UNIV CALIF SAN FRANCISCO,DEPT BIOCHEM & BIOPHYS,SAN FRANCISCO,CA 94143

[3] UNIV CALIF SAN FRANCISCO,DEPT MED,SAN FRANCISCO,CA 94143

[4] EUROPEAN MOLEC BIOL LAB,HAMBURG OUTSTN,HAMBURG,GERMANY

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 173卷 / 02期

关键词：

D O I：

10.1016/S0006-291X(05)80063-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We report a new purification of rabbit reticulocyte 15-lipoxygenase that has resulted in the first crystallization of a mammalian lipoxygenase. The enzyme was purified to homogeneity (greater than 98% pure by SDS-PAGE) using high pressure liquid chromatography on hydrophobic-interaction, hydroxyapatite and cation-exchange columns. Crystals were grown by the vapor diffusion method from concentrated solutions of the protein in sodium phosphate buffer, pH 7.0. The hexagonal, rod-shaped crystals were on average 0.09 mm × 0.09 mm × 0.4 mm, with approximate unit cell dimensions of a=b=260 Å, c=145 Å. The crystals diffract to 5 Å resolution. © 1990 Academic Press, Inc.

引用

页码：507 / 513

页数：7

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