Maguire, Patricia and Ohlendieck, Kay (1996) Oligomerization of sarcoplasmic reticulum Ca2+‐ATPase from rabbit skeletal muscle. FEBS Letters, 396. pp. 115-118. ISSN 0014-5793

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Abstract

Although the primary structure and catalytic cycle of the sarcoplasmic reticulum Ca2+‐ATPase has been revealed, it is not well understood whether functional Ca2+ pump proteins exist in a monomeric or an otigomeric state in native skeletal muscle membranes. Here, we show that the Ca2+‐ATPase tends to form high molecular weight complexes, estimated to be dimers and tetramers using immunoblotting of two‐dimensionally separated microsomal membranes following crosslinking. This agrees with both electron microscopical and biochemical findings which demonstrate that Ca2+‐ATPase clusters are the predominant molecular species in native membranes and that oligomerization may play a role in cooperative kinetics and enzyme stabilization.

Item Type:	Article
Keywords:	Ca2+-ATPase; Sarcoplasmic or endoplasmic reticulum calcium ATPase; Sarcoplasmic reticulum; Skeletal muscle;
Academic Unit:	Faculty of Science and Engineering > Biology
Item ID:	10915
Depositing User:	Prof. Kay Ohlendieck
Date Deposited:	02 Jul 2019 17:03
Journal or Publication Title:	FEBS Letters
Publisher:	Wiley
Refereed:	Yes
URI:
Use Licence:	This item is available under a Creative Commons Attribution Non Commercial Share Alike Licence (CC BY-NC-SA). Details of this licence are available here

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