Author:
Holemans Tine,Vandecaetsbeek Ilse,Wuytack Frank,Vangheluwe Peter
Abstract
The apparent Ca2+ affinity of the isoforms of the sarco/endoplasmic reticulum Ca2+ ATPase SERCA2 is controlled primarily by two proteins, phospholamban (PLB) and sarcolipin (SLN). The rate of ATP-driven Ca2+ uptake into sarcoplasmic reticulum (SR)-derived vesicles can be monitored by a technique in which the net uptake of 45Ca2+ in the form of an intravesicular calcium oxalate precipitate is recorded. Here, we present details of a modification of such a protocol for determining the apparent Ca2+ affinity of the Ca2+ pump, and its control by various regulators, in crude homogenates of mouse heart.
Publisher
Cold Spring Harbor Laboratory
Subject
General Biochemistry, Genetics and Molecular Biology
Cited by
7 articles.
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