Acid-induced uncoupling of sarcoplasmic reticulum membranes is reversed by reconstitution

Mild acid treatment of sarcoplasmic reticulum membranes results in a first order decline in calcium transport activity while calcium stimulated ATPase activity remains unimpaired (Berman, M.C., McIntosh, D.B. and Kench, K.E. (1977) J. Biol. Chem. 252 994–1001). This uncoupling is apparently irrevers...

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Veröffentlicht in:	Biochemical and biophysical research communications 1981-08, Vol.101 (4), p.1426-1432
Hauptverfasser:	Arendse, Michael P., Aderem, Alan A., McIntosh, David B., Berman, Mervyn C.
Format:	Artikel
Sprache:	eng
Schlagworte:	acids Animals Biological Transport, Active Ca(2+) Mg(2+)-ATPase calcium Calcium - metabolism Calcium-Transporting ATPases - metabolism Detergents - pharmacology Intracellular Membranes - metabolism Kinetics Muscles - metabolism Octoxynol Polyethylene Glycols - pharmacology Protein Denaturation Rabbits sarcoplasmic reticulum Sarcoplasmic Reticulum - metabolism Solubility
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Zusammenfassung:	Mild acid treatment of sarcoplasmic reticulum membranes results in a first order decline in calcium transport activity while calcium stimulated ATPase activity remains unimpaired (Berman, M.C., McIntosh, D.B. and Kench, K.E. (1977) J. Biol. Chem. 252 994–1001). This uncoupling is apparently irreversible. Acid inactivated sarcoplasmic reticulum membranes, solubilized with Triton X-100 and reconstituted by passage through a Bio-Bead column, reactivated 80% of the calcium transport activity when compared with untreated, control reconstituted SR vesicles. It is suggested that the inactivated conformation of the (Ca 2+, Mg 2+-)ATPase is constrained by lipid-protein interactions.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/0006-291X(81)91606-5