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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1980-9-26
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pubmed:abstractText |
Treatment of extensively washed erythrocyte membranes with 0.1mm-EDTA decreased their Mg(2+)-dependent, Ca(2+)-stimulated ATPase [(Mg(2+)+Ca(2+))-ATPase] activity. An activator released by this treatment restored the (Mg(2+)+Ca(2+))-ATPase to its original value in a Ca(2+)-dependent manner. This activator was different from calmodulin, as determined by a number of criteria. It was retained on an Amicon XM-100 ultrafiltration membrane (molecular-weight cut-off 100000); it appeared in the void volume of Sephadex G-100 and G-75 columns; it was not retained on a DEAE-cellulose ion-exchange column at ionic strengths similar to those used to retain calmodulin; and it maximally activated (Mg(2+)+Ca(2+))-ATPase activity less than calmodulin and at a higher Ca(2+) concentration. Like calmodulin, the activator is heat-stable. The activator fraction isolated on a 2.5-15% sucrose gradient in 0.16m-KCl showed a single band of mol.wt. 63000 and no calmodulin on 10%-polyacrylamide/sodium dodecyl sulphate gels. A trace amount of calmodulin was detected in the activator fraction by radioimmunoassay (approx. 10pg/ml of ;ghosts'), but this amount was insufficient to account for the (Mg(2+)+Ca(2+))-ATPase activation. Furthermore, calmodulin-binding protein failed to inhibit (Mg(2+)+Ca(2+))-ATPase activity by more than 10-20% in the membrane preparations from which the activator was extracted. It was concluded that erythrocyte membranes contain a (Mg(2+)+Ca(2+))-ATPase activator that may attenuate the activation of the Ca(2+)-transport ATPase by calmodulin.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-1098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-124551,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-14028302,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-144528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-144529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-148293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-148869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-156003,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-156819,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-157356,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-197955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-197956,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-208377,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-4263663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-4326772,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6446908-5806584
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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 |
May
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
187
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
507-13
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:6446908-Blood Proteins,
pubmed-meshheading:6446908-Calcium-Transporting ATPases,
pubmed-meshheading:6446908-Calmodulin,
pubmed-meshheading:6446908-Centrifugation, Density Gradient,
pubmed-meshheading:6446908-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6446908-Enzyme Activation,
pubmed-meshheading:6446908-Erythrocyte Membrane,
pubmed-meshheading:6446908-Erythrocytes,
pubmed-meshheading:6446908-Humans,
pubmed-meshheading:6446908-Magnesium,
pubmed-meshheading:6446908-Membrane Proteins
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pubmed:year |
1980
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pubmed:articleTitle |
A protein activator of Mg2+-dependent, Ca2+-stimulated ATPase in human erythrocyte membranes distinct from calmodulin.
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pubmed:publicationType |
Journal Article
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