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PMID: 6239617 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

A Ca2+-stimulated adenosine triphosphatase in Golgi-enriched membranes of lactating murine mammary tissue.

The Biochemical journal ·Vol. 224 ·No. 1 ·1984-11-15 ·Pages 39-45

Watters CD

Abstract

A membrane fraction isolated from lactating murine mammary tissue and enriched for the Golgi membrane marker enzyme galactosyltransferase exhibited Ca2+-stimulated ATPase activity (Ca-ATPase) in 20 microM-free Mg2+ and 10 microM-MgATP, with an apparent Km for Ca2+ of 0.8 microM. Exogenous calmodulin did not enhance Ca2+ stimulation, nor could Ca-ATPase activities be detected in millimolar total Mg2+ and ATP. When assayed with micromolar Mg2+ and MgATP the Ca-ATPases of skeletal-muscle sarcoplasmic reticulum and of calmodulin-enriched red blood cell plasma membranes were half-maximally activated by 0.1 microM- and 0.6 microM-Ca2+ respectively. All three Ca-ATPases were inhibited by similar micromolar concentrations of trifluoperazine, but the Golgi activity was unaffected by quercetin in concentrations which completely inhibited both the sarcoplasmic-reticulum and red-blood-cell enzymes. The results are consistent with the hypothesis that the high-affinity Ca-ATPase is responsible for the ATP-dependent Ca2+ transport exhibited by Golgi-enriched vesicles derived from lactating mammary gland [Neville, Selker, Semple & Watters (1981) J. Membr. Biol. 61, 97-105; West (1981) Biochim. Biophys. Acta 673, 374-386].

MeSH Terms
Animals Calcium-Transporting ATPases/antagonists & inhibitors,metabolism Calmodulin/pharmacology Enzyme Activation/drug effects Erythrocyte Membrane/enzymology Female Golgi Apparatus/drug effects,enzymology In Vitro Techniques Intracellular Membranes/enzymology Kinetics Lactation Mammary Glands, Animal/enzymology Mice Mice, Inbred Strains Pregnancy Sarcoplasmic Reticulum/enzymology
Chemicals
Calmodulin Calcium-Transporting ATPases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Watters C D
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37 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2240039
Published
1984-11-15
Pages
39-45
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1144395
Subset
IM
Grants
NICHD NIH HHS · HD 14013 · United States
External Links
PubMed source DOI: 10.1042/bj2240039 PMC Full Text View journal details
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