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 | |
| State | Published - 1984 |
| Externally published | Yes |
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Purification and characterization of the naturally occurring allelic variants of sn-glycerol-3-phosphate dehydrogenase in Drosophila Melanogaster. / Bewley, Glenn C.; Niesel, David; 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
}
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
AU - Wilkins, Joseph R.
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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0021727748&partnerID=8YFLogxK
U2 - 10.1016/0305-0491(84)90071-3
DO - 10.1016/0305-0491(84)90071-3
M3 - Article
VL - 79
SP - 23
EP - 32
JO - Comparative biochemistry and physiology. B, Comparative biochemistry
JF - Comparative biochemistry and physiology. B, Comparative biochemistry
SN - 0305-0491
IS - 1
ER -