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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1984-6-14
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pubmed:abstractText |
Purified vitamin D-dependent rat intestinal (Mr 10,000) and rat renal (Mr 28,000) calcium-binding proteins (CaBPs) have been compared to vertebrate calmodulin, and the vitamin D-dependent CaBPs have been found to be distinct from calmodulin by biochemical and immunochemical criteria. Rat renal and rat intestinal CaBPs do not stimulate 3',5'-cyclic nucleotide phosphodiesterase, do not compete with iodinated calmodulin for binding to phenothiazine-Sepharose conjugates, do not cross-react immunochemically, and do not contain N epsilon-trimethyllysine. In addition, although calmodulin exhibits a characteristic calcium-dependent mobility shift on polyacrylamide gels in the presence of sodium dodecyl sulfate, a similar mobility shift is not observed for the vitamin D-dependent CaBPs. Immunocytochemically, calmodulin has a widespread localization in the kidney, whereas CaBP is present specifically in the distal tubules of the kidney. These localizations suggest a specialized role for CaBP in the kidney. Thus, although the vitamin D-dependent CaBPs and calmodulin are similar in that they are small, acidic, calcium-binding proteins, these two classes of proteins are biochemically and immunochemically distinct.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3',5'-Cyclic-AMP Phosphodiesterases,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Protein, Vitamin...,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Phenothiazines
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
231
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
38-47
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:6326677-3',5'-Cyclic-AMP Phosphodiesterases,
pubmed-meshheading:6326677-Amino Acids,
pubmed-meshheading:6326677-Animals,
pubmed-meshheading:6326677-Calcium-Binding Protein, Vitamin D-Dependent,
pubmed-meshheading:6326677-Calcium-Binding Proteins,
pubmed-meshheading:6326677-Calmodulin,
pubmed-meshheading:6326677-Chemical Phenomena,
pubmed-meshheading:6326677-Chemistry,
pubmed-meshheading:6326677-Chickens,
pubmed-meshheading:6326677-Enzyme Activation,
pubmed-meshheading:6326677-Immunochemistry,
pubmed-meshheading:6326677-Immunoenzyme Techniques,
pubmed-meshheading:6326677-Intestines,
pubmed-meshheading:6326677-Kidney,
pubmed-meshheading:6326677-Phenothiazines,
pubmed-meshheading:6326677-Rats
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pubmed:year |
1984
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pubmed:articleTitle |
Calmodulin and rat vitamin D-dependent calcium-binding proteins: biochemical and immunochemical comparison.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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