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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
29
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pubmed:dateCreated |
1992-11-18
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pubmed:abstractText |
A substrate protein for botulinum C3 ADP-ribosyltransferase (C3 exoenzyme) in human platelets was purified to apparent homogeneity from the cytosol by ammonium sulfate fractionation and successive chromatography on columns of DEAE-Sepharose, hydroxylapatite, phenyl-Sepharose, and TSK phenyl-5PW. The purified protein yielded an amino acid sequence identical to that of rhoA protein. When platelet cytosol and membranes were incubated with C3 exoenzyme and [32P]NAD and subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis and isoelectric focusing, they gave only one [32P]ADP-ribosylated band on each electrophoresis that showed an M(r) of 22,000 and a pI of 6.0. The radioactive bands from the two fractions co-migrated with each other and with the [32P]ADP-ribosylated purified protein. When these radioactive products were partially digested with either alpha-chymotrypsin or trypsin and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the same digestion pattern was found in the three samples. These results suggest that the ADP-ribosylation substrate for C3 exoenzyme in the platelet cytosol and membrane is rhoA protein and that it is the sole substrate detectable in human platelets.
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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 |
Oct
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
267
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pubmed:geneSymbol |
rac2,
rho,
rhoA,
rhoB,
rhoC
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20916-20
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:1328215-ADP Ribose Transferases,
pubmed-meshheading:1328215-Adenosine Diphosphate Ribose,
pubmed-meshheading:1328215-Amino Acid Sequence,
pubmed-meshheading:1328215-Blood Platelets,
pubmed-meshheading:1328215-Botulinum Toxins,
pubmed-meshheading:1328215-Cell Membrane,
pubmed-meshheading:1328215-Chromatography,
pubmed-meshheading:1328215-Chromatography, High Pressure Liquid,
pubmed-meshheading:1328215-Chromatography, Ion Exchange,
pubmed-meshheading:1328215-Cytosol,
pubmed-meshheading:1328215-Durapatite,
pubmed-meshheading:1328215-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1328215-GTP-Binding Proteins,
pubmed-meshheading:1328215-Humans,
pubmed-meshheading:1328215-Hydroxyapatites,
pubmed-meshheading:1328215-Molecular Sequence Data,
pubmed-meshheading:1328215-Sequence Homology, Amino Acid,
pubmed-meshheading:1328215-rhoA GTP-Binding Protein
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pubmed:year |
1992
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pubmed:articleTitle |
A rho gene product in human blood platelets. I. Identification of the platelet substrate for botulinum C3 ADP-ribosyltransferase as rhoA protein.
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pubmed:affiliation |
Department of Pharmacology, Kyoto University Faculty of Medicine, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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