| pubmed-article:1454820 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1454820 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
| pubmed-article:1454820 | lifeskim:mentions | umls-concept:C0001443 | lld:lifeskim |
| pubmed-article:1454820 | lifeskim:mentions | umls-concept:C1762617 | lld:lifeskim |
| pubmed-article:1454820 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:1454820 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:1454820 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:1454820 | lifeskim:mentions | umls-concept:C0150312 | lld:lifeskim |
| pubmed-article:1454820 | lifeskim:mentions | umls-concept:C0146894 | lld:lifeskim |
| pubmed-article:1454820 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:1454820 | pubmed:dateCreated | 1993-1-7 | lld:pubmed |
| pubmed-article:1454820 | pubmed:abstractText | In the presence of the nucleotide analog adenosine 5'-[gamma-thio]triphosphate (ATP[gamma S]), effects of Ca2+ on stiffness and equatorial x-ray diffraction patterns of single skinned fibers of the rabbit psoas muscle were studied. It is shown that cross-bridges in the presence of ATP[gamma S] have properties of the weak-binding states of the ATP hydrolysis cycle. Raising the Ca2+ concentration up to pCa 4.5 has little effect on actin affinity of cross-bridges in the presence of ATP[gamma S]. However, the rate constants for cross-bridge dissociation and reassociation from and to actin are reduced by about 2 orders of magnitude. In addition, nucleotide affinity of the cross-bridge is much smaller at high Ca2+ concentrations. Implications for interpretation of fiber stiffness recorded during isotonic shortening and the rising phase of a tetanus are discussed. | lld:pubmed |
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| pubmed-article:1454820 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1454820 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1454820 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1454820 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:1454820 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:1454820 | pubmed:author | pubmed-author:KraftTT | lld:pubmed |
| pubmed-article:1454820 | pubmed:author | pubmed-author:YuL CLC | lld:pubmed |
| pubmed-article:1454820 | pubmed:author | pubmed-author:BrennerBB | lld:pubmed |
| pubmed-article:1454820 | pubmed:author | pubmed-author:KuhnH JHJ | lld:pubmed |
| pubmed-article:1454820 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1454820 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1454820 | pubmed:volume | 89 | lld:pubmed |
| pubmed-article:1454820 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1454820 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1454820 | pubmed:pagination | 11362-6 | lld:pubmed |
| pubmed-article:1454820 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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| pubmed-article:1454820 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1454820 | pubmed:articleTitle | Effect of Ca2+ on weak cross-bridge interaction with actin in the presence of adenosine 5'-[gamma-thio]triphosphate). | lld:pubmed |
| pubmed-article:1454820 | pubmed:affiliation | Department of General Physiology, University of Ulm, Federal Republic of Germany. | lld:pubmed |
| pubmed-article:1454820 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1454820 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:1454820 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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