Amino acid polymorphisms for esterase-6 in Drosophila melanogaster.

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Amino acid polymorphisms for esterase-6 in Drosophila melanogaster.

High-resolution electrophoresis has revealed 10 allozymes of esterase-6 (EC 3.1.1.1) in Drosophila melanogaster. The sequences of 13 isolates of the Est6 gene covering all 10 allozymes were obtained and 52 nucleotide differences were found. Sixteen of these cause amino acid replacements, of which three result in charge differences whose size and direction are consistent with the electrophoretic...

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Clinal variation is common for enzymes in the glycolytic pathway for Drosophila melanogaster and is generally accepted as an adaptive response to different climates. Although the enzyme phosphoglucomutase (PGM) possesses several allozyme polymorphisms, it is unique in that it had been reported to show no clinal variation. Our recent DNA sequence investigation of Pgm found extensive cryptic amin...

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Associations between restriction site polymorphism and enzyme activity variation for esterase 6 in Drosophila melanogaster.

Thirty-five nucleotide polymorphisms were found in a 21.5-kbp region including the Est6 locus among 42 isoallelic lines extracted from a single natural population of Drosophila melanogaster. The heterozygosity per nucleotide pair was estimated to be 0.010 overall, but was lower in sequences hybridizing to transcripts than in those not hybridizing to transcripts. Eleven of 36 pairwise comparison...

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Studies of esterase 6 in Drosophila melanogaster. XVIII. Biochemical differences between the slow and fast allozymes.

Most natural populations of Drosophila melanogaster are polymorphic for two major electrophoretic variants at the esterase-6 locus. The frequency of the EST 6F allozyme is greatest in populations in warmer latitudes, whereas the EST 6S allozyme is predominant in colder latitudes. Latitudinal clines in electromorph frequencies are found on three continents. Purified preparations of the allozymes...

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A Homologous Gene-enzyme System, Esterase 6, in Drosophila Melanogaster and D. Simulans.

HE existence in natural populations of a protein polymorphism involving Ttwo forms of a nonspecific esterase has been established in Drosophila mlamgaster (WRIGHT 1961, 1963). The two forms of the esterase, Esterase 6, are distinguishable by their different electrophoretic mobilities in starch gel, Esterase 6" migrating more rapidly toward the anode than Esterase 6s. The inheritance of these tw...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 1989

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.86.4.1426