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  • Drosophila  (3)
  • affinity chromatography  (1)
  • alcohol dehydrogenase  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Adaptation ofDrosophila enzymes to temperature. III. Evolutionary conservatism in mitochondrial enzymes (1980)
    Springer
    Journal of molecular evolution 16 (1980), S. 37-46 
    Details
    ISSN: 1432-1432
    Keywords: Evolution ; Drosophila ; Temperature ; Mitochondrial enzymes ; Kinetic properties
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The evolutionary behavior of two mitochondrial enzymes (L-glycerol 3-phosphate:cytochrome c oxidoreductase E.C.1.1.1.95,αGPO, and L-malate: NAD+ oxidoreductase, E.C.1.1.1.37, m-MDH) obtained from several temperate and tropicalDrosophila species was examined by comparing their catalytic properties, which related to temperature (Km-Ea-Q10-Thermostability). MitochondrialαGPO or m-MDH obtained either from temperate or from tropical species was found to exhibit similar catalytic properties while for both cytosolic enzymes, theαGPDH and s-MDH, Km patterns were similar among species from the same thermal habitat and different between thermal habitats. In combination with other observations reported in the literature these facts support the view that the function, and probably the structure, of mitochondrial enzymes are better conserved in evolution than those of the corresponding enzymes found in the cytosol. It is proposed that the relative invariance of the mitochondrial enzymes structure is probably linked to a necessary relative invariance of molecular interactions inside the mitochondrion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01732068
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  • 2
    Electronic Resource
    Electronic Resource
    Drosophila lactate dehydrogenase: Molecular and genetic aspects (1982)
    Springer
    Biochemical genetics 20 (1982), S. 1195-1209 
    Details
    ISSN: 1573-4927
    Keywords: lactate dehydrogenase (LDH) ; purification ; affinity chromatography ; LDH molecule characterization ; genetic evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract (LDH) obtained from larvae of Drosophila melanogaster was purified to homogeneity by affinity chromatography on oxamate-Sepharose. The purification procedure is simple to operate and gives a homogeneous preparation in a good yield (34.86%) after only two steps. Utilizing the homogeneous LDH preparation, an attempt was made to characterize the LDH molecule. Thus, it was found that the N-terminal amino acid is isoleucine, and the enzyme is tetrameric and composed of four identical subunits of apparent molecular weight 38,000, suggesting that it is controlled by a single gene. Homogeneous LDH preparations exhibit one band on neutral acrylamide gels when the substrate is either dl-lactic acid or l-(+)-lactate. The optimum temperature is 45°C for the purified enzyme and 40°C for the crude homogenate. The K m values for pyruvate and NADH are 0.154 and 0.027mm, respectively, while the K m values for lactate and NAD are 29.4 and 1.33mm, respectively. A discontinuity in the E a slope was observed at a transition temperature of 30°C. The E a value between 20 and 30°C was calculated as 12.06 kcal/mol, while between 30 and 45°C the E a value was 4.01 kcal/mol. This evidence, together with other observations reported in the literature, suggests that the LDHs of invertebrates and vertebrates have arisen by divergent evolution from a common ancestral gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00498943
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  • 3
    Electronic Resource
    Electronic Resource
    Drosophila lactate dehydrogenase: Developmental aspects (1983)
    Springer
    Biochemical genetics 21 (1983), S. 199-211 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila ; lactate dehydrogenase ; isozymic pattern ; development ; isozymic conversion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Partially purified lactate dehydrogenase (LDH) from third-instar larvae displays two bands (one major and one minor) on polyacrylamide gels. Analogous preparations from pupae and adults exhibit three LDH-staining bands (one major and two minor) in a similar pattern. The migration of the major band is similar for larvae, pupae, and adults, while the two minor LDH bands of pupae and adults migrate more slowly than the minor larval band. It has been shown that larval LDH incubated with β-nicotinamide adenine dinucleotide exhibits two additional minor bands with an electrophoretic mobility similar to that of the minor bands of both pupae and adults. The intensity of the minor larval LDH band (exhibited also by untreated preparations) is drastically reduced. This fact indicates that the life-cycle stage-dependent LDH isozymic distribution is possibly due to a posttranslational effect(s). Highly purified LDH from larvae, pupae, or adults, obtained by an affinity chromatography procedure, displays just one dispersed band, located in the area between the band 5 and the band 6 exhibited by crude extract preparations. These data, in combination with the lack of difference in catalytic properties among enzymes from larvae, pupae, and adults, suggest that LDH synthesis is controlled by the same single structural gene at all developmental stages.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00000018
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  • 4
    Electronic Resource
    Electronic Resource
    Drosophila lactate dehydrogenase: Developmental aspects (1983)
    Springer
    Biochemical genetics 21 (1983), S. 199-211 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila ; lactate dehydrogenase ; isozymic pattern ; development ; isozymic conversion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Partially purified lactate dehydrogenase (LDH) from third-instar larvae displays two bands (one major and one minor) on polyacrylamide gels. Analogous preparations from pupae and adults exhibit three LDH-staining bands (one major and two minor) in a similar pattern. The migration of the major band is similar for larvae, pupae, and adults, while the two minor LDH bands of pupae and adults migrate more slowly than the minor larval band. It has been shown that larval LDH incubated with β-nicotinamide adenine dinucleotide exhibits two additional minor bands with an electrophoretic mobility similar to that of the minor bands of both pupae and adults. The intensity of the minor larval LDH band (exhibited also by untreated preparations) is drastically reduced. This fact indicates that the life-cycle stage-dependent LDH isozymic distribution is possibly due to a posttranslational effect(s). Highly purified LDH from larvae, pupae, or adults, obtained by an affinity chromatography procedure, displays just one dispersed band, located in the area between the band 5 and the band 6 exhibited by crude extract preparations. These data, in combination with the lack of difference in catalytic properties among enzymes from larvae, pupae, and adults, suggest that LDH synthesis is controlled by the same single structural gene at all developmental stages.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02395404
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  • 5
    Electronic Resource
    Electronic Resource
    Enzyme specificity: “pseudopolymorphism” of lactate dehydrogenase in Drosophila melanogaster (1981)
    Springer
    Biochemical genetics 19 (1981), S. 277-299 
    Details
    ISSN: 1573-4927
    Keywords: substrate specificity ; pseudopolymorphism in lactate dehydrogenase ; alcohol dehydrogenase ; Drosophila melanogaster
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract An electrophoretic variant in the LDH (l-lactate:NAD oxidoreductase, E.C.1.1.1.27) of Drosophila melanogaster was observed on starch (or polyacrylamide) gels. This variant was found to exhibit an identical isozymic pattern (three isozymes with a decreasing staining density) on starch gel and map position as the Adh locus. On the other hand, anodal polyacrylamide gel electrophoresis in crude extracts has shown LDH to consist of nine bands and ADH of four bands. We have shown that ADH (Alcohol:NAD oxidoreductase, E.C.1.1.1.1) also oxidizes l(+)-lactate or d(−)-lactate with the NAD, while LDH oxidizes ethanol. By using various genetic and biochemical techniques, we have shown that the observed Ldh electrophoretic variant was not a real one and could be attributed to the presence of ADH. We have called this phenomenon “pseudopolymorphism,” and the problem of enzyme specificity has been examined. The appearance of a band in an assay using lactic acid as a substrate is not sufficient evidence for the presence of LDH. Hence, caution is called for before characterizing an electrophoretic band on a gel as being equivalent to the presence of a genetic locus. Out of the nine electrophoretic zones of activity observed on polyacrylamide gel (or out of the six previously observed) using crude extract, only two (one major and one minor) belong to LDH, as revealed by purified enzyme preparations. Furthermore, purified LDH exhibits activity in two bands on starch gel (out of three observed in crude extracts), which appear in different positions as compared with those of ADH. Finally, one band which responds to the presence of d(−)-lactate but not to l(+)-lactate has been revealed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00504274
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