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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
43
|
| pubmed:dateCreated |
1994-12-1
|
| pubmed:databankReference | |
| pubmed:abstractText |
NAD:arginine ADP-ribosyltransferases catalyze the ADP-ribosylation of arginine residues in proteins. Coding region nucleic acid and deduced amino acid sequences of a human skeletal muscle ADP-ribosyltransferase cDNA were, respectively, 80.8% and 81.3% identical to those of the rabbit skeletal muscle transferase. A human transferase-specific cDNA probe detected major mRNA of 1.2 kb (mouse and rat), 3.0 kb (rabbit), 3.8 kb (monkey), and 5.7 kb (human) upon Northern analysis. Polyclonal anti-rabbit ADP-ribosyltransferase antibodies reacted with 36,000 M(r) proteins in partially purified transferase preparations from bovine, dog, and rabbit heart muscle and a 40,000 M(r) protein from human skeletal muscle. The human muscle ADP-ribosyltransferase cDNA, like the previously cloned rabbit muscle transferase, predicts predominantly hydrophobic amino- and carboxy-terminal amino acid sequences, which is characteristic of glycosylphosphatidylinositol (GPI)-anchored proteins. On immunoblots of partially purified rabbit and human skeletal muscle ADP-ribosyltransferases, anti-cross-reacting determinant antibodies detected at 36,000 and 40,000 M(r), respectively, phosphatidylinositol-specific, phospholipase C-sensitive, GPI-anchored proteins. These data are consistent with the conclusion that GPI-anchored skeletal and cardiac muscle ADP-ribosyltransferases are conserved across mammalian species.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP Ribose Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Probes,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Diester Hydrolases
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0006-2960
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
33
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
12828-36
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7947688-ADP Ribose Transferases,
pubmed-meshheading:7947688-Amino Acid Sequence,
pubmed-meshheading:7947688-Animals,
pubmed-meshheading:7947688-Base Sequence,
pubmed-meshheading:7947688-Conserved Sequence,
pubmed-meshheading:7947688-DNA Probes,
pubmed-meshheading:7947688-Glycosylphosphatidylinositols,
pubmed-meshheading:7947688-Humans,
pubmed-meshheading:7947688-Immunoblotting,
pubmed-meshheading:7947688-Mammary Neoplasms, Experimental,
pubmed-meshheading:7947688-Molecular Sequence Data,
pubmed-meshheading:7947688-Muscle, Skeletal,
pubmed-meshheading:7947688-Myocardium,
pubmed-meshheading:7947688-Phosphatidylinositol Diacylglycerol-Lyase,
pubmed-meshheading:7947688-Phosphoric Diester Hydrolases,
pubmed-meshheading:7947688-Rabbits,
pubmed-meshheading:7947688-Rats,
pubmed-meshheading:7947688-Sequence Homology,
pubmed-meshheading:7947688-Tumor Cells, Cultured
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferases.
|
| pubmed:affiliation |
Laboratory of Cellular Metabolism, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.
|
| pubmed:publicationType |
Journal Article,
Comparative Study
|