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)|
|Number of pages||10|
|Journal||Comparative Biochemistry and Physiology -- Part B: Biochemistry and|
|State||Published - 1984|
ASJC Scopus subject areas
- Molecular Biology