@article{f283789355d348cea632ed9436de3847,
title = "Purification and characterization of the naturally occurring allelic variants of sn-glycerol-3-phosphate dehydrogenase in Drosophila Melanogaster",
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.",
author = "Bewley, {Glenn C.} and Niesel, {David W.} and Wilkins, {Joseph R.}",
note = "Funding Information: The well-defined role of GPDH in insect metabolism has prompted intensive genetic and biochemical investigation into this gene--enzyme system in Drosophila melanogaster. The enzyme activity consists of a family of three isozymes, designated as GPDH-1, -2, and -3, which are uniquely distributed with respect to developmental and tissue specific expression (reviewed by Bewley, 1983). GPDH-1 is largely restricted to adult thoracic flight muscle where it participates in the glycerolphosphate cycle. GPDH-3 is most abundant in larval fat body and the internal abdominal tissues of the adult. These two major isozymes have been purified to homogeneity and demonstrated to be functionally dimeric with a subunit size of M, = 32,000 (Miller and Berger, 1979; *Paper No. 9178 of the Journal Series of the North Carolina Agricultural Research Service, Raleigh, NC 27650. This project has been supported by Public Health Service Research Grants GM-23617 and AG-01739 to G.C.B. tPresent address: Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77550, U.S.A.",
year = "1984",
doi = "10.1016/0305-0491(84)90071-3",
language = "English (US)",
volume = "79",
pages = "23--32",
journal = "Comparative Biochemistry and Physiology -- Part B: Biochemistry and",
issn = "0305-0491",
publisher = "Elsevier B.V.",
number = "1",
}