A profile of Drosophila species' enzymes assayed by electrophoresis. I. Number of alleles, heterozygosities, and linkage disequilibrium in glucose-metabolizing systems and some other enzymes (original) (raw)

Abstract

Seven isolated large populations of Drosophila belonging to five different species were examined by starch gel electrophoresis for allozyme variation. Six to eleven enzyme loci in the glucose-metabolizing system (group I) and six to eight enzyme loci (group II) which were not directly involved in the above-mentioned system were assayed. The parameters estimated were the average number of alleles per locus, allele frequencies, proportions of polymorphic loci, and average heterozygosity per population for group I and group II loci. The major finding is that genetic variability measured by allozyme variations is much higher for group II than for group I enzymes in terms of every parameter in all the populations. This is consistent with the earlier findings in D. ananassae by Gillespie and Kojima (1968). Linkage disequilibrium, a measure of genome integration, was computed between an enzyme locus and an inversion segment of the same chromosome. The preliminary analysis of this aspect of the study indicates that no substantial linkage disequilibrium builds up between the chromosomal segments unless the pair of segments is less than 10 centimorgan units apart.

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Authors and Affiliations

  1. Department of Zoology, University of Texas at Austin, Austin, Texas
    Ken-ichi Kojima & John Gillespie
  2. Department of Biology, Tokyo Metropolitan University, Tokyo, Japan
    Yoshiko N. Tobari

Authors

  1. Ken-ichi Kojima
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  2. John Gillespie
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  3. Yoshiko N. Tobari
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Additional information

This study was supported by USPHS Grant GM-15769 and Atomic Energy Commission Contract AT-(40-1)-3681.

NIH Trainee supported by Grant 5 TO 1 GM 00337.

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Kojima, Ki., Gillespie, J. & Tobari, Y.N. A profile of Drosophila species' enzymes assayed by electrophoresis. I. Number of alleles, heterozygosities, and linkage disequilibrium in glucose-metabolizing systems and some other enzymes.Biochem Genet 4, 627–637 (1970). https://doi.org/10.1007/BF00486100

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