Structural analysis of glycerol-3-phosphate dehydrogenase from severalDrosophila species
Chambers, G. K. ; Felton, A. A. ; Ramshaw, J. A. M. ; Rigby, D. Larson ; Sullivan, D. T.
Springer
Published 1985
Springer
Published 1985
| ISSN: |
1573-4927
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| Keywords: |
Drosophila melanogaster ; D. hydei ; D. immigrans ; D. mercatorum ; glycerol-3-phosphate dehydrogenase ; peptide mapping ; amino acid sequencing
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| Source: |
Springer Online Journal Archives 1860-2000
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| Topics: |
Biology
Chemistry and Pharmacology
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| Notes: |
Abstract This report describes preliminary protein structural studies of glycerol-3-phosphate dehydrogenase (α-GPDH) fromDrosophila spp. and an important innovative feature of our enzyme purification protocol. The scheme involves the coupling of substrate (α-glycerophosphate) elution from CM-Sephadex and cofactor (NADH) elution from Affi-Gel blue resin. Using this method a 32.7% yield and a 111-fold purification were obtained from aD. melanogaster line carrying the α-Gpdh S allele at the α-Gpdh locus. The product obtained from 0 to 3-day-old adult flies was electrophoretically homogeneous and consisted mainly of the adult α-GPDH-1 isozyme. The method was used to obtain α-GPDH protein fromD. melanogaster (two lines),D. hydei, D. immigrans, andD. mercatorum. Peptide mapping revealed structural differences among the enzymes from the different species, and amino acid sequencing showed many similarities betweenD. melanogaster α-GPDH and the rabbit muscle enzyme.
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| Type of Medium: |
Electronic Resource
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| URL: |