DIFFERENT THERMOSTABILITIES OF SARCOPLASMIC-RETICULUM (CA2++MG2+)-ATPASES FROM RABBIT AND TROUT MUSCLES

被引：7

作者：

DETOLEDO, FGS

ALBUQUERQUE, MC

GOULART, BH

CHINI, EN

机构：

[1] MAYO CLIN & MAYO FDN,DIV NEPHROL,NEPHROL RES UNIT,ROCHESTER,MN 55905

[2] MAYO CLIN & MAYO FDN,DEPT PHYSIOL & INTERNAL MED,ROCHESTER,MN 55905

[3] UNIV FED RIO DE JANEIRO,ILHA FDN,INST CIENCIAS BIOMED,DEPT BIOQUIM,BR-21945 RIO JANEIRO,BRAZIL

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY C-PHARMACOLOGY TOXICOLOGY & ENDOCRINOLOGY | 1995年 / 111卷 / 01期

关键词：

(CA2+ + MG2+)-ATPASE; MUSCLE; RABBIT; SARCOPLASMIC RETICULUM; TEMPERATURE ADAPTATION; RAINBOW TROUT; CONFORMATIONAL STATES;

D O I：

10.1016/0742-8413(95)00017-2

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：

Trout and rabbit (Ca2+ + Mg2+)-ATPases from sarcoplasmic reticulum were compared for differences in thermal inactivation and susceptibility to trypsin digestion, The trout ATPase is more heat-sensitive than the rabbit ATPase and is stabilized by Ca2+, Na+, K+ and nucleotides, Solubilization of both ATPases shows that the two ATPases have different protein-intrinsic inactivation kinetics, When digested by trypsin, the two ATPases display different cleavage patterns, The present results indicate that the trout and rabbit ATPases have dissimilarities in protein structure that may explain the differences in thermal inactivation kinetics.

引用

页码：93 / 98

页数：6

共 21 条

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