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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
16
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pubmed:dateCreated |
1982-10-12
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pubmed:abstractText |
Nonmuscle, smooth muscle, and striated muscle tissue extracts contain several proteins, in addition to calmodulin, which bind fluphenazine affinity columns in a calcium-dependent manner. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis shows four proteins in red blood cell lysates with Mr = 22,000, 12,000, 9,000, and 8,000. Rat brain tissue contains an 11,000-dalton peptide, while chicken gizzard and rabbit longissimus dorsi muscles have a similar set of peptides (67,000, 35,000, 33,000, and 11,000 daltons). These proteins all interact independently with fluphenazine and, except for the 22,000-dalton protein from red blood cells, do not bind to calmodulin-Sepharose affinity columns. Binding requires the presence of micromolar calcium, and dissociation occurs only by chelation of calcium with EDTA or ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid. The muscle tissue proteins are present in ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid eluates from N-(6-aminohexyl)-5-chloro-1-naphthalene sulfonamide- and phenothiazine-coupled Sepharose resins but are not bound to a Sepharose column without a coupled drug. These results suggest that the use of phenothiazines to indicate calmodulin action should be judiciously interpreted. These proteins may be functionally analogous to calmodulin in that they form a drug-binding site in a calcium-dependent manner.
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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/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Fluphenazine,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
257
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9663-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7107584-Animals,
pubmed-meshheading:7107584-Blood Proteins,
pubmed-meshheading:7107584-Brain Chemistry,
pubmed-meshheading:7107584-Calcium,
pubmed-meshheading:7107584-Calcium-Binding Proteins,
pubmed-meshheading:7107584-Calmodulin,
pubmed-meshheading:7107584-Chickens,
pubmed-meshheading:7107584-Chromatography, Affinity,
pubmed-meshheading:7107584-Fluphenazine,
pubmed-meshheading:7107584-Muscle, Smooth,
pubmed-meshheading:7107584-Muscle Proteins,
pubmed-meshheading:7107584-Muscles,
pubmed-meshheading:7107584-Protein Binding,
pubmed-meshheading:7107584-Proteins,
pubmed-meshheading:7107584-Rabbits,
pubmed-meshheading:7107584-Rats
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pubmed:year |
1982
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pubmed:articleTitle |
Calcium-dependent protein binding to phenothiazine columns.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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