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

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

Research output: Contribution to journalArticle

9 Scopus citations

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

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology

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