| pubmed-article:2139345 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2139345 | lifeskim:mentions | umls-concept:C0036226 | lld:lifeskim |
| pubmed-article:2139345 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:2139345 | lifeskim:mentions | umls-concept:C1413043 | lld:lifeskim |
| pubmed-article:2139345 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:2139345 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2139345 | pubmed:dateCreated | 1990-5-25 | lld:pubmed |
| pubmed-article:2139345 | pubmed:abstractText | Vanadate-sensitized photocleavage of the Ca2(+)-ATPase of rabbit sarcoplasmic reticulum was observed upon illumination of sarcoplasmic reticulum vesicles or the purified Ca2(+)-ATPase by ultraviolet light in the presence of 1 mM monovanadate or decavanadate. The site of the photocleavage is influenced by the Ca2+ concentration of the medium. When the [Ca2+] is maintained below 10 nM by EGTA, the vanadate-catalyzed photocleavage yields fragments of approximately equal to 87 and approximately equal to 22 kDa, while in the presence of 2-20 mM Ca, polypeptides of 71 and 38 kDa are obtained as the principal cleavage products. These observations indicate that the site of the vanadate-catalyzed photocleavage is altered by changes in the conformation of Ca2(+)-ATPase. Selective tryptic proteolysis, at Arg-505-Ala-506, combined with covalent labeling of Lys-515 by fluorescein 5'-isothiocyanate and with the use of anti-ATPase antibodies of defined specificity, permitted the tentative allocation of the sites of photocleavage to the A fragment near the T2 cleavage site in the absence of Ca2+, and to the B fragment between Lys-515 and Asp-659 in the presence of 2-20 mM Ca2+. The loss of ATPase activity during illumination is accelerated by calcium in the presence of vanadate. The vanadate-catalyzed photocleavage in the presence of Ca2+ is consistent with the existence of an ATPase-Ca2(+)-vanadate complex (Markus et al. (1989) Biochemistry 28, 793-799). | lld:pubmed |
| pubmed-article:2139345 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139345 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2139345 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139345 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2139345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139345 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139345 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2139345 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:2139345 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:2139345 | pubmed:author | pubmed-author:MartonosiAA | lld:pubmed |
| pubmed-article:2139345 | pubmed:author | pubmed-author:MolnarEE | lld:pubmed |
| pubmed-article:2139345 | pubmed:author | pubmed-author:VegaTT | lld:pubmed |
| pubmed-article:2139345 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2139345 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:2139345 | pubmed:volume | 1023 | lld:pubmed |
| pubmed-article:2139345 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2139345 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2139345 | pubmed:pagination | 168-83 | lld:pubmed |
| pubmed-article:2139345 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:meshHeading | pubmed-meshheading:2139345-... | lld:pubmed |
| pubmed-article:2139345 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2139345 | pubmed:articleTitle | Vanadate-catalyzed, conformationally specific photocleavage of the Ca2(+)-ATPase of sarcoplasmic reticulum. | lld:pubmed |
| pubmed-article:2139345 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, State University of New York, Syracuse 13210. | lld:pubmed |
| pubmed-article:2139345 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2139345 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2139345 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:2139345 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
