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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1980-6-27
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pubmed:abstractText |
Calcium uptake by adipocyte endoplasmic reticulum was studied in a rapidly obtained microsomal fraction. The kinetics and ionic requirements of Ca2+ transport in this preparation were characterized and compared to those of (Ca2+ + Mg2+)-ATPase activity. The time course of Ca2+ uptake in the presence of 5 mM oxalate was nonlinear, approaching a steady-state level of 10.8--11.5 nmol Ca2+/mg protein after 3--4 min of incubation. The rate of Ca2+ transport was iM oxalate. The calculated initial rate of calcium uptake was 18.5 nmol Ca2+/mg protein per min. The double reciprocal plot of ATP concentration against transport rate was nonlinear, with apparent Km values of 100 muM and 7 muM for ATP concentration ranges above and below 50 muM, respectively. The apparent Km values for Mg2+ and Ca2+ were 132 muM and 0.36--0.67 muM, respectively. The energy of activation was 23.4 kcal/mol. These kinetic properties were strikingly similar to those of the microsomal (Ca2+ + Mg2+)-ATPase. The presence of potassium was required for maximum Ca2+ transport activity. The order of effectiveness of monovalent cations in stimulating both Ca2+ transport and (Ca2+ + Mg2+)-ATPase activity was K+ greater than Na+ = NH4+ greater than Li+. Ca2+ transport and (Ca2+ + Mg2+)-ATPase activity were both inhibited 10--20% by 6 mM procaine and less than 10% by 10 mM sodium azide. Both processes were completely inhibited by 3 mM dibucaine or 50 muM p-chloromercuribenzene sulfonate. The results indicate that Ca2+ transport in adipocyte endoplasmic reticulum is mediated by a (Ca2+ + Mg2+)-ATPase and suggest an important role for endoplasmic reticulum in control of intracellular Ca2+ distribution.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ca(2 ) Mg(2 )-ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Transporting ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Monovalent,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Oxalates
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
596
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
359-71
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:6102477-Adipose Tissue,
pubmed-meshheading:6102477-Animals,
pubmed-meshheading:6102477-Biological Transport, Active,
pubmed-meshheading:6102477-Ca(2+) Mg(2+)-ATPase,
pubmed-meshheading:6102477-Calcium,
pubmed-meshheading:6102477-Calcium-Transporting ATPases,
pubmed-meshheading:6102477-Cations, Monovalent,
pubmed-meshheading:6102477-Endoplasmic Reticulum,
pubmed-meshheading:6102477-Kinetics,
pubmed-meshheading:6102477-Magnesium,
pubmed-meshheading:6102477-Male,
pubmed-meshheading:6102477-Oxalates,
pubmed-meshheading:6102477-Rats
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pubmed:year |
1980
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pubmed:articleTitle |
Relationship between calcium ion transport and (Ca2+ + Mg2+)-atpase activity in adipocyte endoplasmic reticulum.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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