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

doi:10.1016/S0003-9861(71)80018-8

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

Department of Biology

Research output: Contribution to journal › Article

31 Scopus citations

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 language	English (US)
Pages (from-to)	583-590
Number of pages	8
Journal	Archives of Biochemistry and Biophysics
Volume	145
Issue number	2
DOIs	https://doi.org/10.1016/S0003-9861(71)80018-8
State	Published - Aug 1971

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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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.",

author = "Fondy, {Thomas P.} and Herwig, {Kenneth J.} and Sollohub, {Susan J.} and Rutherford, {Diane Barr}",

year = "1971",

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AU - Rutherford, Diane Barr

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