Isolation and structural properties of cytoplasmic glycerol-3-phosphate dehydrogenase from rat liver

Thomas P Fondy, Kenneth J. Herwig, Susan J. Sollohub, Diane Barr Rutherford

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Cytoplasmic, NAD-linked l-glycerol-3-P dehydrogenase (EC 1.1.1.8) was shown to exist as a single major isoenzymic from in the livers of 120-200-g rats when fresh homogenates were examined by polyacrylamide gel isoelectric focusing. The enzyme was isolated in apparently homogenous form and the amino acid composition established. The molecular weight estimated by gel filtration was 63.000±6,000.

Original languageEnglish (US)
Pages (from-to)583-590
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume145
Issue number2
DOIs
StatePublished - Jan 1 1971

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Glycerolphosphate Dehydrogenase
Isoelectric Focusing
Liver
NAD
Glycerol
Gel Chromatography
Rats
Structural properties
Oxidoreductases
Molecular Weight
Gels
Molecular weight
Amino Acids
Enzymes
Chemical analysis
polyacrylamide gels

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Isolation and structural properties of cytoplasmic glycerol-3-phosphate dehydrogenase from rat liver. / Fondy, Thomas P; Herwig, Kenneth J.; Sollohub, Susan J.; Rutherford, Diane Barr.

In: Archives of Biochemistry and Biophysics, Vol. 145, No. 2, 01.01.1971, p. 583-590.

Research output: Contribution to journalArticle

Fondy, Thomas P ; Herwig, Kenneth J. ; Sollohub, Susan J. ; Rutherford, Diane Barr. / Isolation and structural properties of cytoplasmic glycerol-3-phosphate dehydrogenase from rat liver. In: Archives of Biochemistry and Biophysics. 1971 ; Vol. 145, No. 2. pp. 583-590.
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