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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1993-2-10
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pubmed:abstractText |
Single-channel properties of a polypeptide fraction from the nematode Caenorhabditis elegans highly enriched in binding sites were studied in planar bilayers. [3H]Ryanodine binding sites were purified by sucrose gradient centrifugation of C. elegans microsomes solubilized in CHAPS detergent. The highest [3H]ryanodine binding activity sedimented at approximately 18% sucrose (wt/vol), and was composed of a major polypeptide with a M(r) of 360,000 and a minor polypeptide with a M(r) of 170,000. The ryanodine-binding polypeptide(s) formed a Ca(2+)-permeable channel with a permeability ratio P(divalent)/P(monovalent) = 4 and two conductance states of 215 pS and 78 pS in 0.25 M KCl. Ryanodine locked the channel in the 78 pS state and inhibited transitions between the 215 pS and 78 pS states. These data demonstrated the presence of a ryanodine receptor in C. elegans with functional properties comparable to those described in mammalian muscle.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-1302004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-139159,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-1648106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-1648939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-1652123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-2169916,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-2380170,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-2448641,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-2459298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-2459777,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-2463249,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-2469164,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-2537473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-2694942,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-2725677,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-3355834,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-3985981,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-4366476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-4887724,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-5839255,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-6040534,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1335783-7190524
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-3495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
63
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1379-84
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1335783-Animals,
pubmed-meshheading:1335783-Binding Sites,
pubmed-meshheading:1335783-Biophysical Phenomena,
pubmed-meshheading:1335783-Biophysics,
pubmed-meshheading:1335783-Caenorhabditis elegans,
pubmed-meshheading:1335783-Calcium Channels,
pubmed-meshheading:1335783-Helminth Proteins,
pubmed-meshheading:1335783-Kinetics,
pubmed-meshheading:1335783-Molecular Weight,
pubmed-meshheading:1335783-Muscle Proteins,
pubmed-meshheading:1335783-Receptors, Cholinergic,
pubmed-meshheading:1335783-Ryanodine,
pubmed-meshheading:1335783-Ryanodine Receptor Calcium Release Channel
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pubmed:year |
1992
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pubmed:articleTitle |
High molecular weight proteins in the nematode C. elegans bind [3H]ryanodine and form a large conductance channel.
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pubmed:affiliation |
Department of Physiology, School of Medicine, University of Wisconsin, Madison 53706.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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