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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1985-1-3
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pubmed:abstractText |
The naturally occurring electrophoretic variants of sn-glycerol-3-phosphate dehydrogenase and a heterodimeric form of the enzyme resulting from a genetic cross of two variant strains of Drosophila were purified to homogeneity by a combination of DEAE-cellulose chromatography and 8-(6-aminohexyl)-amino-ATP-Sepharose affinity chromatography. Each purified protein was compared with respect to a number of physicochemical and kinetic properties. All forms of the enzyme were found to be similar, except for pI differences associated with the electrophoretic variation observed.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0305-0491
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
79
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23-32
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6437737-Amino Acids,
pubmed-meshheading:6437737-Animals,
pubmed-meshheading:6437737-Chromatography, Affinity,
pubmed-meshheading:6437737-Chromatography, DEAE-Cellulose,
pubmed-meshheading:6437737-Drosophila melanogaster,
pubmed-meshheading:6437737-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6437737-Glycerolphosphate Dehydrogenase,
pubmed-meshheading:6437737-Isoelectric Point,
pubmed-meshheading:6437737-Kinetics
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pubmed:year |
1984
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pubmed:articleTitle |
Purification and characterization of the naturally occurring allelic variants of sn-glycerol-3-phosphate dehydrogenase in Drosophila melanogaster.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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