PURIFICATION AND PROPERTIES OF A (CA-2++MG-2+)-ATPASE FROM POTAMON-POTAMIOS SKELETAL-MUSCLE SARCOPLASMIC-RETICULUM

被引：5

作者：

TENTES, I ^{[1
]}

PATERAKI, L ^{[1
]}

STRATAKIS, E ^{[1
]}

机构：

[1] UNIV CRETE,DEPT BIOL,IRAKLION,GREECE

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1992年 / 103卷 / 04期

关键词：

D O I：

10.1016/0305-0491(92)90208-9

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：

1. A 120-kDa (Ca2+ + Mg2+)-dependent ATPase was purified from the freshwater/land crab Potamon potamios muscle sarcoplasmic reticulum. 2. The enzyme showed two K(m) values for ATP of 40 and 330 mM at 10-75 and >75 muM ATP concentrations, respectively. K(m) values for calcium and magnesium were 2 and 294 muM, respectively. 3. Optimal enzyme activity was observed at pH 7.5 and the Arrhenius plot showed a break at 25-degrees-C. 4. An alternative method for the simultaneous purification of P. potamios (Ca2+ + Mg2+)- and (Na+ + K+)-dependent ATPase enzymes is also described.

引用

页码：875 / 880

页数：6

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