Purification and characterization of the naturally occurring allelic variants of sn-glycerol-3-phosphate dehydrogenase in Drosophila Melanogaster

Glenn C. Bewley; David W. Niesel; Joseph R. Wilkins

doi:10.1016/0305-0491(84)90071-3

Purification and characterization of the naturally occurring allelic variants of sn-glycerol-3-phosphate dehydrogenase in Drosophila Melanogaster

Glenn C. Bewley
, David W. Niesel
, Joseph R. Wilkins

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

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)
Pages (from-to)	23-32
Number of pages	10
Journal	Comparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume	79
Issue number	1
DOIs	https://doi.org/10.1016/0305-0491(84)90071-3
State	Published - 1984
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Physiology
Molecular Biology

Access to Document

10.1016/0305-0491(84)90071-3

Cite this

Purification and characterization of the naturally occurring allelic variants of sn-glycerol-3-phosphate dehydrogenase in Drosophila Melanogaster. / Bewley, Glenn C.; Niesel, David W.; Wilkins, Joseph R.
In: Comparative Biochemistry and Physiology -- Part B: Biochemistry and, Vol. 79, No. 1, 1984, p. 23-32.

Research output: Contribution to journal › Article › peer-review

@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",

}

TY - JOUR

T1 - Purification and characterization of the naturally occurring allelic variants of sn-glycerol-3-phosphate dehydrogenase in Drosophila Melanogaster

AU - Bewley, Glenn C.

AU - Niesel, David W.

AU - Wilkins, Joseph R.

N1 - 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.

PY - 1984

Y1 - 1984

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0021727748

UR - https://www.scopus.com/pages/publications/0021727748#tab=citedBy

U2 - 10.1016/0305-0491(84)90071-3

DO - 10.1016/0305-0491(84)90071-3

M3 - Article

C2 - 6437737

AN - SCOPUS:0021727748

SN - 0305-0491

VL - 79

SP - 23

EP - 32

JO - Comparative Biochemistry and Physiology -- Part B: Biochemistry and

JF - Comparative Biochemistry and Physiology -- Part B: Biochemistry and

IS - 1

ER -

Purification and characterization of the naturally occurring allelic variants of sn-glycerol-3-phosphate dehydrogenase in Drosophila Melanogaster

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this