Purification and characterization of the naturally occurring allelic variants of sn-glycerol-3-phosphate dehydrogenase in Drosophila Melanogaster

Glenn C. Bewley, David Niesel, Joseph R. Wilkins

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

1. 1. The naturally occurring electrophoretic variants of sn-glycerol-3-phosphate dehydrogenase and a heterodimetric 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. 2. 2. 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.

Original languageEnglish (US)
Pages (from-to)23-32
Number of pages10
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume79
Issue number1
DOIs
StatePublished - 1984
Externally publishedYes

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Glycerolphosphate Dehydrogenase
Drosophila melanogaster
Purification
Genetic Crosses
Affinity chromatography
DEAE-Cellulose Chromatography
DEAE-Cellulose
Agarose Chromatography
Enzymes
Chromatography
Affinity Chromatography
Drosophila
Kinetics
Proteins
ATP-sepharose

ASJC Scopus subject areas

  • Medicine(all)

Cite this

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AU - Bewley, Glenn C.

AU - Niesel, David

AU - Wilkins, Joseph R.

PY - 1984

Y1 - 1984

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