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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
1981-12-15
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pubmed:abstractText |
The sulfhydryl groups of tubulin are reported to play a role in regulating microtubule assembly and colchicine binding to tubulin. The alkylating agents iodo[14C]acetamide and its bifunctional analogue N,N'-ethylenebis(iodoacetamide) are used as probes for the sulfhydryl groups of tubulin. In the presence of 8 M urea, alpha- and beta-tubulin have 10-11 and 8 alkylatable sulfhydryls, respectively, and one of the high molecular weight proteins (HMW 2) has 5 sulfhydryls/Mr 271 000. In the absence of urea, the rates of alkylation of alpha- and beta-tubulin are significantly lower but that of HMW 2 is unaffected. The sulfhydryls of tubulin are masked in intact microtubules. N,N'-Ethylenebis(iodoacetamide) reacts with free tubulin to generate a band, designated beta, which migrates ahead of beta on polyacrylamide gels. beta appears to represent a form of beta-tubulin containing at least one intrachain cross-link between sulfhydryl groups. Formation of beta* is inhibited in intact microtubules and is abolished if tubulin is denatured by 8 M urea, 1% sodium dodecyl sulfate, or boiling. N,N'-Ethylenebis(iodoacetamide) may thus be used as a probe for the native conformation of free tubulin.
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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/Alkylating Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Ethylenediamines,
http://linkedlifedata.com/resource/pubmed/chemical/Iodoacetamide,
http://linkedlifedata.com/resource/pubmed/chemical/Iodoacetates,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Tubulin
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4437-44
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7284333-Alkylating Agents,
pubmed-meshheading:7284333-Animals,
pubmed-meshheading:7284333-Brain,
pubmed-meshheading:7284333-Carbon Radioisotopes,
pubmed-meshheading:7284333-Cattle,
pubmed-meshheading:7284333-Cross-Linking Reagents,
pubmed-meshheading:7284333-Ethylenediamines,
pubmed-meshheading:7284333-Iodoacetamide,
pubmed-meshheading:7284333-Iodoacetates,
pubmed-meshheading:7284333-Kinetics,
pubmed-meshheading:7284333-Microtubules,
pubmed-meshheading:7284333-Peptide Fragments,
pubmed-meshheading:7284333-Protein Binding,
pubmed-meshheading:7284333-Tubulin
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pubmed:year |
1981
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pubmed:articleTitle |
Interaction of tubulin with drugs and alkylating agents. 1. Alkylation of tubulin by iodo[14C]acetamide and N,N'-ethylenebis(iodoacetamide).
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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