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 language | English (US) |
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Pages (from-to) | 23-32 |
Number of pages | 10 |
Journal | Comparative Biochemistry and Physiology -- Part B: Biochemistry and |
Volume | 79 |
Issue number | 1 |
DOIs | |
State | Published - 1984 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Physiology
- Molecular Biology