Calcium Regulation in Heart Cells
- 1 August 1976
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 67 (2), 389-396
- https://doi.org/10.1111/j.1432-1033.1976.tb10703.x
Abstract
A study was carried out of the interaction of dog heart mitochondria and sarcoplasmic reticulum with Ca2+ bound to troponin or to its Ca2+-binding component (troponin-C). Both organelles are able to release more than 80% of the Ca2+ bound to the 2 proteins. Sarcoplasmic reticulum is only able to do so in the presence of oxalate, whereas mitochondria are also active in the absence of permeant Ca-complexing anions. Ca2+ uptake in heart mitochondria is severely inhibited by Mg2+. The results are discussed with reference to the problem of the control of Ca2+ in heart sarcoplasm.This publication has 41 references indexed in Scilit:
- Characterization of Cardiac Sarcoplasmic Reticulum ATP‐ADP Phosphate Exchange and Phosphorylation of the Calcium Transport Adenosine TriphosphataseEuropean Journal of Biochemistry, 1976
- An in vitro study of the interaction of heart mitochondria with troponin-bound Ca2+Biochemical and Biophysical Research Communications, 1975
- Ionized magnesium concentration in axoplasm of dialyzed squid axonsFEBS Letters, 1975
- Binding and Release of Cations by Sarcoplasmic Reticulum before and after Removal of LipidEuropean Journal of Biochemistry, 1972
- The effect of ruthenium red on Ca2+ transport and respiration in rat liver mitochondriaBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1972
- Separation and characterization of the constituents of troponinFEBS Letters, 1971
- Specific inhibition of mitochondrial Ca++ transport by ruthenium redBiochemical and Biophysical Research Communications, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- COMPARATIVE ULTRASTRUCTURE AND CALCIUM TRANSPORT IN HEART AND SKELETAL MUSCLE MICROSOMESThe Journal of cell biology, 1969
- The site of diphosphoinositide synthesis in rat liverBiochemical and Biophysical Research Communications, 1965