| pubmed-article:2521860 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2521860 | lifeskim:mentions | umls-concept:C0036226 | lld:lifeskim |
| pubmed-article:2521860 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:2521860 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:2521860 | lifeskim:mentions | umls-concept:C0324026 | lld:lifeskim |
| pubmed-article:2521860 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2521860 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2521860 | pubmed:dateCreated | 1989-3-28 | lld:pubmed |
| pubmed-article:2521860 | pubmed:abstractText | Scallop sarcoplasmic reticulum (SR), visualized in situ by freeze-fracture and deep-etching, is characterized by long tubes displaying crystalline arrays of Ca2+-ATPase dimer ribbons, resembling those observed in isolated SR vesicles. The orderly arrangement of the Ca2+-ATPase molecules is well preserved in muscle bundles permeabilized with saponin. Treatment with saponin, however, is not needed to isolate SR vesicles displaying a crystalline surface structure. Omission of ATP from the isolation procedure of SR vesicles does not alter the dimeric organization of the Ca2+-ATPase, although the overall appearance of the tubes seems to be affected: the edges of the vesicles are scalloped and the individual Ca2+-ATPase molecules are not clearly defined. The effect of Ca2+ on isolated scallop SR vesicles was investigated by correlating the enzymatic activity and calcium-binding properties of the Ca2+-ATPase with the surface structure of the vesicles, as revealed by electron microscopy. The dimeric organization of the membrane is preserved at Ca2+ concentrations where the Ca2+ binds to the high affinity sites (half-maximum saturation at pCa approximately 7.0 with a Hill coefficient of 2.1) and the Ca2+-ATPase is activated (half-maximum activation at pCa approximately 6.8 with a Hill coefficient of 1.84). Higher Ca2+ concentrations disrupt the crystalline surface array of the SR tubes, both in the presence and absence of ATP. We discuss here whether the Ca2+-ATPase dimer identified as a structural unit of the SR membrane represents the Ca2+ pump in the membrane. | lld:pubmed |
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| pubmed-article:2521860 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2521860 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2521860 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2521860 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:2521860 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:2521860 | pubmed:author | pubmed-author:HardwickeP... | lld:pubmed |
| pubmed-article:2521860 | pubmed:author | pubmed-author:CastellaniLL | lld:pubmed |
| pubmed-article:2521860 | pubmed:author | pubmed-author:Franzini-Arms... | lld:pubmed |
| pubmed-article:2521860 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2521860 | pubmed:volume | 108 | lld:pubmed |
| pubmed-article:2521860 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2521860 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2521860 | pubmed:pagination | 511-20 | lld:pubmed |
| pubmed-article:2521860 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:2521860 | pubmed:meshHeading | pubmed-meshheading:2521860-... | lld:pubmed |
| pubmed-article:2521860 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2521860 | pubmed:articleTitle | Effect of Ca2+ on the dimeric structure of scallop sarcoplasmic reticulum. | lld:pubmed |
| pubmed-article:2521860 | pubmed:affiliation | Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254-9110. | lld:pubmed |
| pubmed-article:2521860 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2521860 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2521860 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:2521860 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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