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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1986-5-16
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pubmed:abstractText |
In our previous study [Chalovich, J. M., Greene, L. E., & Eisenberg, E. (1983) Proc. Natl. Acad. Sci. U.S.A. 80, 4909-4913], myosin subfragment 1 that was modified by having its two reactive thiol groups cross-linked by N,N'-p-phenylenedimaleimide (pPDM) was found to resemble the myosin subfragment 1-adenosine 5'-triphosphate (S-1.ATP) complex in its interaction with actin. In the present study, we examined the effect of actin on adenosine 5'-diphosphate (ADP) trapped at the active site of pPDM.S-1. Our results indicate first that, in the presence of actin, ADP is no longer trapped at the active site but exchanges rapidly with free nucleotide. Different pPDM.S-1.nucleotide complexes were then formed by exchanging nucleotide into the active site of pPDM.S-1 in the presence of actin. The binding of pPDM.S-1.ATP or pPDM.S-1.PPi to actin is virtually identical with that of unmodified S-1 in the presence of ATP. Specifically, at mu = 18 mM, 25 degrees C, pPDM.S-1.ATP or pPDM.S-1.PPi binds to unregulated actin with the same affinity as does S-1.ATP, and this binding does not appear to be affected by troponin-tropomyosin. On the other hand, pPDM.S-1.ADP and pPDM.S-1 with no bound nucleotide both show a small, but significant, difference between their binding to actin and the binding of S-1.ATP; pPDM.S-1 and pPDM.S-1.ADP both bind about 2- to 3-fold more strongly to unregulated actin than does S-1.ATP.(ABSTRACT TRUNCATED AT 250 WORDS)
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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/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Maleimides,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Subfragments,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins,
http://linkedlifedata.com/resource/pubmed/chemical/N,N'-2-phenylenedimaleimide,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
704-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:3955026-Actins,
pubmed-meshheading:3955026-Adenosine Diphosphate,
pubmed-meshheading:3955026-Adenosine Triphosphate,
pubmed-meshheading:3955026-Binding Sites,
pubmed-meshheading:3955026-Carbon Radioisotopes,
pubmed-meshheading:3955026-Kinetics,
pubmed-meshheading:3955026-Maleimides,
pubmed-meshheading:3955026-Myosin Subfragments,
pubmed-meshheading:3955026-Myosins,
pubmed-meshheading:3955026-Peptide Fragments,
pubmed-meshheading:3955026-Protein Binding,
pubmed-meshheading:3955026-Tritium
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pubmed:year |
1986
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pubmed:articleTitle |
Effect of nucleotide on the binding of N,N'-p-phenylenedimaleimide-modified S-1 to unregulated and regulated actin.
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pubmed:publicationType |
Journal Article
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