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Journal ArticleDOI

The effect of anti-ATPase antibodies upon the Ca++ transport of sarcoplasmic reticulum

TLDR
Antibodies prepared against the Ca ++ binding protein (C 1 protein) have no influence upon either ATPase activity or Ca ++ transport and ferritin-labeled anti-C 1 antibodies do not bind to microsomes.
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This article is published in Biochemical and Biophysical Research Communications.The article was published on 1974-09-09. It has received 37 citations till now. The article focuses on the topics: Plasma membrane Ca2+ ATPase & ATPase.

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Citations
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Journal ArticleDOI

Effect of the lipid environment on protein motion and enzymatic activity of sarcoplasmic reticulum calcium ATPase.

TL;DR: The modification of the lipid phase of the enzyme, observed the effects on the enzymatic activity at low temperatures, and correlated these effects with spectroscopic measurements of the rotational motions of both the lipid and protein components are consistent with the proposal that both lipid fluidity and protein rotational mobility are essential for enzyme activity.
Journal ArticleDOI

Immunochemical quantification of sarcoplasmic reticulum Ca-ATPase, of calsequestrin and of parvalbumin in rabbit skeletal muscles of defined fiber composition

TL;DR: Antibodies directed against purified Ca-ATPase from sarcoplasmic reticulum, calsequestrin and parvalbumin from rabbit fast-twitch muscle were raised in sheep and suggest a fiber-type-specific polymorphism of the sarcoplASPase, which is found to be 6-7 times higher in fast than in slow-twitch muscles.
Journal ArticleDOI

The sarcoplasmic reticulum Ca2+-ATPase.

TL;DR: Studies on the structural organization of Ca2+-ATPase in the sarcoplasmic reticulum membrane in relation to the function of the transport protein suggest that breaks in Arrhenius plots of enzyme activity primarily reflect intrinsic properties of the protein rather than changes in the character of lipid motion as a function of temperature.
Journal ArticleDOI

Large-scale rotational motions of proteins detected by electron paramagnetic resonance and fluorescence.

TL;DR: Saturation transfer spectroscopy (ST-EPR), a recently developed EPR technique that permits the detection of rotational correlation times as long as 1 ms, has been used to detect large-scale rotational motions of spin-labeled proteins in muscle filaments and in membranes, providing valuable insights into energy transduction mechanisms in these assemblies.
References
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Journal ArticleDOI

Voltage Dependent Charge Movement in Skeletal Muscle: a Possible Step in Excitation–Contraction Coupling

TL;DR: It is suggested that a link in excitation-contraction coupling involves the movement of a fixed amount of charge free to move between different locations across the membrane.
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Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum

TL;DR: An adenosine triphosphatase has been purified approximately 6-fold from sarcoplasmic reticulum through the use of deoxycholate and salt fractionation and the rate of ATP-ADP exchange and the level of phosphorylation are both increased by a factor commensurate with the increase in ATPase activity.
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The structure of erythrocyte membranes studied by freeze-etching. II. Localization of receptors for phytohemagglutinin and influenza virus to the intramembranous particles.

TL;DR: Results provide further support for the idea that membrane-bound glycoproteins are oriented so that their carbohydrate-rich segments, which bear the antigenic sites and receptors, are exposed to the external medium, while hydrophobic segments of the same molecules interact with lipids, and possibly other proteins, to form the intramembranous particles.
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