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. 1984 Dec 1;224(2):445–451. doi: 10.1042/bj2240445

Evidence for the presence in smooth muscle of two types of Ca2+-transport ATPase.

F Wuytack, L Raeymaekers, J Verbist, H De Smedt, R Casteels
PMCID: PMC1144451  PMID: 6151392

Abstract

Membrane fractions prepared from smooth muscle of the pig stomach (antral part) contain two Ca2+-dependent phosphoprotein intermediates belonging to different Ca2+-transport ATPases. These alkali-labile phosphoproteins can be separated by electrophoresis in acid medium. The 130 kDa phosphoprotein resembles a corresponding protein in the erythrocyte membrane, whereas the 100 kDa protein resembles that of the Ca2+-transport ATPase in sarcoplasmic reticulum from skeletal muscle. These resemblances are expressed in terms of Mr, reaction to La3+ and in a similar proteolytic degradation pattern. The presence of the calmodulin-stimulated ATPase in mixed membranes from smooth muscle is confirmed by its binding of calmodulin and antibodies against erythrocyte Ca2+-transport ATPase, whereas such binding does not occur with proteins present in the presumed endoplasmic reticulum from smooth muscle.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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