Biochemical comparison of arginine kinase allozymes in Drosophila melanogaster

Yi-Chih Chien, Glen E. Collier

Research output: Contribution to journalArticle

Abstract

Biochemical comparison of arginine kinase allozymes in Drosophila melanogaster. Zoological Studies 36(4): 277-287. ARKB is a rare arginine kinase allozyme found in natural populations of Drosophila melanogaster. To test whether the rarity of this allozyme could be due to its biochemical impairment relative to the common allozyme, biochemical properties such as catalytic efficiency and conformational stability of the rare (ARKB) and the common (ARKA) allozymes were compared in this study. Both allozymes were purified by ammonium sulfate fractionation, DEAE-ion-exchange column, Blue-Sepharose, and S-300 gel filtration, to yield a single coomassie-blue band on SDS-polyacrylamide gels. ARKA has a higher Vmax or Vmax/Km than ARKB at 18 or 29 °C, but there are no differences at 24 °C. In general, ARKA is catalytically more efficient than ARKB. Heat treatment of the allozymes shows that ARKB has a lower specific activity than ARKA, and its temperature of heat inactivation is also lower. Also, the rate of heat inactivation of ARKB is faster. Therefore, ARKB is more thermolabile than ARKA. From comparisons of catalytic efficiency and thermal stability of the allozymes, we assume that ARKB is biochemically less efficient than ARKA, and that might partially account for the rarity of ArgkB in natural populations of D. melanogaster.

Original languageEnglish
Pages (from-to)277-287
Number of pages11
JournalZoological Studies
Volume36
Issue number4
Publication statusPublished - 1997 Oct 1

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allozymes
Drosophila melanogaster
heat inactivation
catalytic activity
gels
arginine kinase
ion exchange
polyacrylamide
thermal stability
ammonium sulfate
agarose
fractionation
heat treatment
temperature

All Science Journal Classification (ASJC) codes

  • Animal Science and Zoology

Cite this

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abstract = "Biochemical comparison of arginine kinase allozymes in Drosophila melanogaster. Zoological Studies 36(4): 277-287. ARKB is a rare arginine kinase allozyme found in natural populations of Drosophila melanogaster. To test whether the rarity of this allozyme could be due to its biochemical impairment relative to the common allozyme, biochemical properties such as catalytic efficiency and conformational stability of the rare (ARKB) and the common (ARKA) allozymes were compared in this study. Both allozymes were purified by ammonium sulfate fractionation, DEAE-ion-exchange column, Blue-Sepharose, and S-300 gel filtration, to yield a single coomassie-blue band on SDS-polyacrylamide gels. ARKA has a higher Vmax or Vmax/Km than ARKB at 18 or 29 °C, but there are no differences at 24 °C. In general, ARKA is catalytically more efficient than ARKB. Heat treatment of the allozymes shows that ARKB has a lower specific activity than ARKA, and its temperature of heat inactivation is also lower. Also, the rate of heat inactivation of ARKB is faster. Therefore, ARKB is more thermolabile than ARKA. From comparisons of catalytic efficiency and thermal stability of the allozymes, we assume that ARKB is biochemically less efficient than ARKA, and that might partially account for the rarity of ArgkB in natural populations of D. melanogaster.",
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Biochemical comparison of arginine kinase allozymes in Drosophila melanogaster. / Chien, Yi-Chih; Collier, Glen E.

In: Zoological Studies, Vol. 36, No. 4, 01.10.1997, p. 277-287.

Research output: Contribution to journalArticle

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