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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1982-5-21
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pubmed:abstractText |
The emergence of the reactivity of -SH groups associated with conformation changes has been studied on the ADP/ATP carrier, is isolated in three different inhibitor-protein complexes. 1. The bongkrekate-protein complex incorporates approximately one molecular more of N-ethylmaleimide than the carboxyatractylate-protein complex. After extensive denaturation by dodecylsulfate in urea, both inhibitor complexes exhibit four reactive -SH groups per subunit. Thus one of four -SH groups per subunit has been unmasked in the bongkrekate-protein complex. 2. The interconversion from the bongkrekate-protein complex to the carboxyatractylate-protein complex is inhibited after the -SH groups have been blocked. 3. The protein complex isolated with the more easily dissociable atractylate, is used to demonstrate, by the emergence of the -SH groups, the transition into the m-state. This transition is specifically catalyzed by ADP and ATP. 4. Using 2,2'-dinitro-5,5'-dithiodibenzoate, the appearance of the -SH groups on transition from the c-state to the m-state can be followed spectrophotometrically. The specificity for the catalyzing nucleotides is identical with that for the transport. The Km for ADP and ATP is in the range of 1 microM. In conclusion, the thiol groups of the isolated ADP/ATP carrier behave as in the mitochondrial membrane. The unmasking of -SH groups is in full accordance with the concept of two conformational states (c and m).
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Bongkrekic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial ADP, ATP Translocases,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/carboxyatractylate-binding...
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
122
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
141-5
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:6277631-Adenosine Diphosphate,
pubmed-meshheading:6277631-Animals,
pubmed-meshheading:6277631-Bongkrekic Acid,
pubmed-meshheading:6277631-Carrier Proteins,
pubmed-meshheading:6277631-Cattle,
pubmed-meshheading:6277631-Kinetics,
pubmed-meshheading:6277631-Mitochondria, Heart,
pubmed-meshheading:6277631-Mitochondrial ADP, ATP Translocases,
pubmed-meshheading:6277631-Nucleotidyltransferases,
pubmed-meshheading:6277631-Sulfhydryl Compounds,
pubmed-meshheading:6277631-Time Factors
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pubmed:year |
1982
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pubmed:articleTitle |
The reactivity of -SH groups in the ADP/ATP carrier isolated from beef heart mitochondria.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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