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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 |
1990-5-25
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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).
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Transporting ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Egtazic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescein-5-isothiocyanate,
http://linkedlifedata.com/resource/pubmed/chemical/Fluoresceins,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Free Radicals,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Thiocyanates,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/Vanadates
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
1023
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
168-83
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:2139345-Animals,
pubmed-meshheading:2139345-Antibodies,
pubmed-meshheading:2139345-Antibodies, Monoclonal,
pubmed-meshheading:2139345-Calcium,
pubmed-meshheading:2139345-Calcium-Transporting ATPases,
pubmed-meshheading:2139345-Egtazic Acid,
pubmed-meshheading:2139345-Fluorescein-5-isothiocyanate,
pubmed-meshheading:2139345-Fluoresceins,
pubmed-meshheading:2139345-Fluorescent Dyes,
pubmed-meshheading:2139345-Free Radicals,
pubmed-meshheading:2139345-Molecular Weight,
pubmed-meshheading:2139345-Muscles,
pubmed-meshheading:2139345-Oxygen,
pubmed-meshheading:2139345-Photochemistry,
pubmed-meshheading:2139345-Protein Conformation,
pubmed-meshheading:2139345-Rabbits,
pubmed-meshheading:2139345-Sarcoplasmic Reticulum,
pubmed-meshheading:2139345-Thiocyanates,
pubmed-meshheading:2139345-Trypsin,
pubmed-meshheading:2139345-Ultraviolet Rays,
pubmed-meshheading:2139345-Vanadates
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pubmed:year |
1990
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pubmed:articleTitle |
Vanadate-catalyzed, conformationally specific photocleavage of the Ca2(+)-ATPase of sarcoplasmic reticulum.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, State University of New York, Syracuse 13210.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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