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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1987-6-11
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pubmed:abstractText |
We investigated the endogenous mono(ADP-ribosyl)ation of the sarcoplasmic reticulum from rabbit skeletal muscle. The autoradiogram obtained after sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the [adenylate-32P]NAD-treated sarcoplasmic reticulum vesicles revealed a major band corresponding to the MW 105 K Ca2+-dependent ATPase and other bands corresponding to proteins of MW 153, 60 and 38 K and those of 125 to 135 K range. The addition of poly L-lysine during the incubation led to an enhancement of the modification. Poly L-lysine is proving to be a pertinent tool for identifying acceptor proteins.
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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 |
Apr
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
144
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
856-62
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:2953340-Adenosine Diphosphate Ribose,
pubmed-meshheading:2953340-Animals,
pubmed-meshheading:2953340-Arginine,
pubmed-meshheading:2953340-Calcium-Transporting ATPases,
pubmed-meshheading:2953340-Kinetics,
pubmed-meshheading:2953340-Muscles,
pubmed-meshheading:2953340-NADP,
pubmed-meshheading:2953340-Phosphates,
pubmed-meshheading:2953340-Polylysine,
pubmed-meshheading:2953340-Rabbits,
pubmed-meshheading:2953340-Sarcoplasmic Reticulum
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pubmed:year |
1987
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pubmed:articleTitle |
Mono(ADP-ribosyl)ation of Ca2+-dependent ATPase in rabbit skeletal muscle sarcoplasmic reticulum and the effect of poly L-lysine.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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