CONVERSION OF BASAL 6.0 S ADENYLATE-CYCLASE INTO 7.4 S BY GUANYL NUCLEOTIDE TREATMENT OF MEMBRANE-BOUND ENZYME

被引：23

作者：

GUILLON, G

COURAUD, PO

ROY, C

机构：

[1] Laboratoire de Physiologie Cellulaire Collège de France

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 87卷 / 03期

关键词：

D O I：

10.1016/0006-291X(79)92036-9

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：

Membrane-bound adenylate cyclase from pig kidney medulla was pretreated with either guanyl-5′-yl-imidodiphosphate (Gpp(NH)p) or NaF and solubilized in the presence of Triton X100 (0.7 % v v). Pretreatment by Gpp(NH)p, but not by NaF, shifted the standard sedimentation constant of the solubilized enzyme from 6.0 S to 7.4 S. This effect depended on the Gpp(NH)p concentration used and correlated to the nucleotide-induced increase in adenylate cyclase catalytic activity. Both the 6.0 S and 7.4 S activity peaks had similar Stokes radii. © 1979.

引用

页码：855 / 861

页数：7

共 19 条

[1] IRREVERSIBLE ACTIVATION OF ADENYLATE-CYCLASE OF TOAD ERYTHROCYTE PLASMA-MEMBRANE BY 5'-GUANYLYLIMIDODIPHOSPHATE [J].