Sarcoplasmic reticulum Ca2+-ATPase activity in cod (Gadus morhua) muscle measured in crude homogenates

被引：6

作者：

Godiksen, H ^{[1
]}

Jessen, F ^{[1
]}

机构：

[1] Tech Univ Denmark, Dept Seafood Res, Danish Inst Fisheries Res, DK-2800 Lyngby, Denmark

来源：

JOURNAL OF FOOD BIOCHEMISTRY | 2001年 / 25卷 / 04期

关键词：

D O I：

10.1111/j.1745-4514.2001.tb00744.x

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：

An assay for sarcoplasmic reticulum Ca2+-ATPase in an unfractionated homogenate from cod (Gadus morhua) muscle has been established Specificity of the assay was demonstrated by the Ca2+ dependence of the enzyme and the effect of a specific inhibitor, thapsigargin. Stimulation and inhibition of enzyme activity was observed at low and high Ca2+ concentration, respectively. Half the maximal activity was obtained at 0.2 muM free calcium and no activity could be detected above 20 mM free Ca2+. Thapsigargin inhibited 92% of enzyme activity. Sarcoplasmic reticulum Ca2+-ATPase showed maximal activity around pH 7 and 25C A nonlinear Arrhenius plot was found with pronounced changes in the slope in the temperature interval 6-15C The activation energies obtained from the approximately linear parts above 15C and below 6C were 25 kJ mol(-1) and 172 kJ mol(-1), respectively.

引用

页码：343 / 358

页数：16

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