EVIDENCE FOR 2 DISTINCT ATP SITES IN NA,K-ATPASE PURIFIED FROM PIG-KIDNEY

被引：0
作者：
WARD, DG
SCHONER, W
CAVIERES, JD
机构：
[1] UNIV LEICESTER,DEPT CELL PHYSIOL & PHARMACOL,LEICESTER LE1 9HN,LEICS,ENGLAND
[2] UNIV GIESSEN,INST BIOCHEM & ENDOKRINOL,FACHBEREICHS VET MED,W-6300 GIESSEN,GERMANY
来源：
JOURNAL OF PHYSIOLOGY-LONDON | 1994年 / 480P卷
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D O I：
暂无
中图分类号：
Q189 [神经科学];
学科分类号：
071006 ;
摘要：
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页码：P84 / P84
页数：1
相关论文
共 2 条
[1]   SHIFT TO THE NA+ FORM OF NA+/K+-TRANSPORTING ATPASE DUE TO MODIFICATION OF THE LOW-AFFINITY ATP-BINDING SITE BY CO(NH3)4ATP [J].
SCHEINERBOBIS, G ;
ESMANN, M ;
SCHONER, W .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1989, 183 (01) :173-178
[2]   SOLUBILIZED ALPHA-BETA NA,K-ATPASE REMAINS PROTOMERIC DURING TURNOVER YET SHOWS APPARENT NEGATIVE COOPERATIVITY TOWARD ATP [J].
WARD, DG ;
CAVIERES, JD .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (11) :5332-5336
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