The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Calcium Binding and ATPase Activities of Heart Sarcolemma
Naranjan S. DHALLAMadhu B. ANANDJames A. C. HARROW
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1976 年 79 巻 6 号 p. 1345-1350

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Rat heart sarcolemma prepared by the hypotonic shock-LiBr treatment method was found to bind calcium by a concentration-dependent and saturable process. The calcium binding values at 50μM and 1.25mM Ca2+ concentrations were about 30 and 250nmoles/mg protein, respectively. Both Mg2+ and ATP inhibited calcium binding and no evidence for energy-linked calcium binding with sarcolemma was found. On the other hand, maximal ATP hydrolysis by heart sarcolemma was seen at 4mM Mg2+ or Ca2+. The Ca2+-ATPase [EC 3.6.1.3] activity was depressed by the presence of Mg2+ or excess ATP. Low concentrations (10-100μM) of Ca2+ failed to stimulate ATP hydrolysis in the presence of various concentrations of Mg-ATP. These results indicate the absence of a “calcium pump” mechanism in the heart sarcolemmal membrane preparation employed in this study.

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© The Japanese Biochemical Society
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