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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2 Pt 2
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pubmed:dateCreated |
1989-3-23
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pubmed:abstractText |
Enriched plasma membrane preparations of the branchial epithelium of freshwater-adapted eels were used to study adenosine triphosphatase (ATPase) activities insensitive to ouabain and responding to Ca2+ and Mg2+. Ca2+ induced ATP hydrolysis; two kinetics were observed in the presence or absence of chelators, one with a high-affinity site (0.3 microM) and one with a lower affinity site (10-20 microM). The high-affinity Ca2+ site or enzyme had a prerequisite for Mg2+ (endogenous Mg2+ being sufficient to satisfy the Mg2+ need) but was inhibited by exogenous Mg2+ (Ki0.5 less than 10 microM Mg2+). The low-affinity site or enzyme appears to have kinetic parameters comparable to those found for Mg2+-induced ATP hydrolysis. In the absence of Ca2+ ligands and with no exogenous Mg2+, the two Ca2+ sites or enzymes can be considered stimulated. The results are discussed in relation to the branchial ion environment and transport ion capacities.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0002-9513
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
256
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
R313-22
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:2537036-Anguilla,
pubmed-meshheading:2537036-Animals,
pubmed-meshheading:2537036-Ca(2+) Mg(2+)-ATPase,
pubmed-meshheading:2537036-Calcium-Transporting ATPases,
pubmed-meshheading:2537036-Egtazic Acid,
pubmed-meshheading:2537036-Gills,
pubmed-meshheading:2537036-Kinetics,
pubmed-meshheading:2537036-Magnesium,
pubmed-meshheading:2537036-Magnesium Chloride,
pubmed-meshheading:2537036-Nitrilotriacetic Acid,
pubmed-meshheading:2537036-Ouabain,
pubmed-meshheading:2537036-Sodium-Potassium-Exchanging ATPase
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pubmed:year |
1989
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pubmed:articleTitle |
Ca2+-stimulated ATPase activities in the gill of the eel: interactions of Mg2+ ions.
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pubmed:affiliation |
Laboratoire Jean Maetz, Departement de Biologie du Commissariat à l'Energie Atomique, Villefranche-sur-Mer, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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