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  • Articles  (10)
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  • isozymes  (10)
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  • 1970-1974  (10)
  • Chemistry and Pharmacology  (10)
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  • Articles  (10)
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  • Springer  (10)
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  • 1
    Electronic Resource
    Electronic Resource
    Properties of alcohol dehydrogenase isozymes in a strain of Drosophila melanogaster homozygous for the Adh-slow allele (1974)
    Springer
    Biochemical genetics 11 (1974), S. 167-175 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; alcohol dehydrogenase ; isozymes ; conformers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Two isozymes of alcohol dehydrogenase from Drosophila melanogaster homozygous for the Adh-slow allele have been separated by isoelectric focusing. The isozymes differ in their temperature optima, temperature stabilities, specific activities, and at least one of their Michaelis constants. They are immunologically identical. Evidence is presented that NAD may partially convert one isozyme into another. The possible nature of these isozymic differences is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485772
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  • 2
    Electronic Resource
    Electronic Resource
    Biochemical genetics of hybrid sunfish: Differential survival of heterozygotes (1974)
    Springer
    Biochemical genetics 11 (1974), S. 205-219 
    Details
    ISSN: 1573-4927
    Keywords: heterosis ; heterozygosity ; hybrids ; isozymes ; sunfish ; Centrarchidae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Allelic segregation in reciprocal backcrosses involving the largemouth bass (Micropterus salmoides) and the F1 hybrid (largemouth bass × smallmouth bass, M. dolomieui) was investigated to determine the extent of euheterosis and luxuriance. The frequencies of allelic isozymes encoded in the lactate dehydrogenase E, malate dehydrogenase B, and isocitrate dehydrogenase loci were determined for reciprocal backcross progeny subjected to different selection pressures. The progeny of the backcross (male F1 × female largemouth bass) underwent a rapid loss of heterozygous individuals in a natural pond environment. When the offspring of this same mating were placed in artificial pools, where cannibalism is the main source of mortality, heterozygosity was advantageous. There was a marked correlation of increased heterozygosity at these enzyme loci with an increased growth rate. None of the above responses to selection was observed when the F1 hybrid served as the maternal parent in the reciprocal backcross. A maternal factor in the egg cytoplasm may influence the expression of heterosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486056
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  • 3
    Electronic Resource
    Electronic Resource
    Genetic study of pancreatic proteinase and α-amylase in mice (Mus musculus) (1974)
    Springer
    Biochemical genetics 12 (1974), S. 419-428 
    Details
    ISSN: 1573-4927
    Keywords: mice ; isozymes ; pancreas ; proteinase ; α-amylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Genetic variants were found at two loci for pancreatic proteinase in mice. The Prt-1 locus contains a pair of allelic genes, Prt-1 a and Prt-1 b , ad the Prt-2 locus contains two codominant allelic genes, Prt-2 a and Prt-2 b .Expression of the two genetic variants of proteinase allowed mice strains used in this study to be classified into three phenotypic classes. Prt-1 b andPrt-2 a were found in most of the Japanese inbred strains, Prt-1 b andPrt-2 a were found in most of the inbred strains imported from the United States, and, furthermore, Prt-1 b and Prt-2 b were present in Japanese feral-origin mice strains. Prt-1, Prt-2, and Amy-2 loci did not belong to the same linkage group.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486646
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  • 4
    Electronic Resource
    Electronic Resource
    Properties of genetically polymorphic isozymes of alcohol dehydrogenase in Drosophila melanogaster (1974)
    Springer
    Biochemical genetics 11 (1974), S. 141-153 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; alcohol dehydrogenase ; isozymes ; allozymes ; polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Studies of the isozymes produced by alternative alleles at the alcohol dehydrogenase locus of Drosophila melanogaster indicate that the ADH F enzyme is more active but less stable than the ADHS enzyme. The difference in stability is manifested in the responses to various conditions of temperature, pH, and protein concentration. The two enzymes also appear to differ in their substrate specificities. It is clear that the differences of primary structure involved in the ADH polymorphism can have profound effects on the biological activity of the molecule.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485770
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  • 5
    Electronic Resource
    Electronic Resource
    The relative quantities and catalytic activities of enzymes produced by alleles at the alcohol dehydrogenase locus in Drosophila melanogaster (1974)
    Springer
    Biochemical genetics 11 (1974), S. 155-165 
    Details
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; alcohol dehydrogenase ; isozymes ; enzyme kinetics ; polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract We have examined the kinetic properties of enzymes produced by the electrophoretically fast (F) and slow (S) alleles at the alcohol dehydrogenase locus in a polymorphic laboratory population of Drosophila melanogaster. The product of the F allele has approximately twice the specific activity of the product of the S allele. We have estimated four Michaelis constants (K ethanol, K NAD, K′ethanol, and K′NAD) and have found no significant difference between the major (ADH-5) isozyme produced by homozygotes for the two alleles. The relative amounts of enzyme produced by the homozygotes were estimated by the method of Laurell (1966), and again no significant differences were found. It appears that the difference in specific activities can be explained solely in terms of relative catalytic efficiency. In a series of laboratory stocks, those fixed for the F allele tend to produce more enzyme than those fixed for the S allele. These observations do not support the view that the alleles are selectively equivalent.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485771
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  • 6
    Electronic Resource
    Electronic Resource
    Sunflower alcohol dehydrogenase: ADH1 genetics and dissociation-recombination (1974)
    Springer
    Biochemical genetics 11 (1974), S. 17-24 
    Details
    ISSN: 1573-4927
    Keywords: Helianthus annuus ; alcohol dehydrogenase ; isozymes ; dissociation-recombination ; genetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The composite alcohol dehydrogenase zymogram of sunflowers, Helianthus annuus, consists of 12 distinct bands. Genetic studies suggest that the slowest-moving three bands are allozymic dimers. They are controlled by a gene designated Adh 1 having two codominant alleles, Adh 1 F and Adh 1 S . The heterozygote produces three bands as expected with a dimer molecule, while the homozygotes produce but one band each, consisting of FF or SS homodimers. The genetic evidence is supported by dissociation-recombination experiments in which the homodimers were separated and allowed to rejoin as parental homodimers and the hybrid heterodimer. Adh 1 FS was found in only three of 422 cultivar seeds of one collection out of about 70 (over 6000 individual seeds tested) and was seen only infrequently in the seven wild collections examined. Adh 1 SS has never been found in the cultivar collections studied and but rarely in the wild populations sampled.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486615
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  • 7
    Electronic Resource
    Electronic Resource
    Electrophoretic variation of supernatant malate dehydrogenase in marsupials (1974)
    Springer
    Biochemical genetics 11 (1974), S. 25-32 
    Details
    ISSN: 1573-4927
    Keywords: malate dehydrogenase ; isozymes ; marsupials
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Starch gel electrophoresis of supernatant malate dehydrogenase (MDH A2) was performed on erythrocyte samples from 505 individual animals representative of 33 marsupial species. Most species exhibited electrophoretically identical forms of MDH A2 activity with the exception of the grey kangaroos, Trichosurus possums, and bandicoots, thus confirming the phylogenetic relatedness of animals within each group and the conservative nature of this enzyme. Polymorphisms were observed in two of the six species analyzed whose mobilities were non-standard. Allelic isozyme patterns and those from interspecies F1 hybrids between grey kangaroos and other macropods were consistent with a dimeric subunit structure and an autosomal locus (MDH-A) encoding the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486616
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  • 8
    Electronic Resource
    Electronic Resource
    Analysis of human erythrocyte glucose 6-phosphate dehydrogenase isozymes by isoelectric focusing in polyacrylamide gel (1974)
    Springer
    Biochemical genetics 12 (1974), S. 51-58 
    Details
    ISSN: 1573-4927
    Keywords: glucose 6-phosphate dehydrogenase ; erythrocytes ; isozymes ; isoelectric focusing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The method of isoelectric focusing in polyacrylamide gel was used to separate G6PD isozymes in crude hemolysates of human, rabbit, and rat erythrocytes. G6PD (B) from erythrocytes of a normal human male donor revealed six bands of activity. Their mean isoelectric points, using pH 3–10 and 5–8 range empholytes, were pI 7.04 for band I, pI 6.60 for band II, pI 6.37 for band III, pI 6.11 for band IV, pI 5.94 for band V, pI 5.79 for band VI. G6PD from rabbit and rat erythrocytes revealed completely different multiple band patterns. The method of isoelectric focusing in polyacrylamide gel is presented as a new way of detecting G6PD isozyme patterns.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00487527
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  • 9
    Electronic Resource
    Electronic Resource
    Leaf peroxidase activities in tomato mutants affecting plant morphology (1974)
    Springer
    Biochemical genetics 12 (1974), S. 181-198 
    Details
    ISSN: 1573-4927
    Keywords: Lycopersicon esculentum ; peroxidases ; isozymes ; genetic control
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The leaf peroxidase activity and the electrophoretic banding pattern of 69 tomato mutants affecting plant morphology have been studied. The zymograms of 63 mutants were normal, and their total peroxidase activities were not correlated with a particular plant or leaf trait. However, six mutations, lyrate x-1521, mottled, olivacea, monstrosa, extreme dwarf, and Curl, are characterized by one or two isozymic bands more intensely stained than in the normal electrophoretic pattern; concomitantly, their total peroxidase activities increase significantly, reaching, in the mutant olivacea, a value forty fold higher than in nonmutant stocks. These abnormal levels of total peroxidase activity are achieved by a promotion of the constitutive bands A5 or C2, singularly or simultaneously. It may be inferred that the six abovementioned mutations influence directly or indirectly the peroxidase activity level without affecting the genes which code for the peroxidase isozymes themselves. Parallels between the mutant effects on specific peroxidase bands and hormonally mediated control of the peroxidase isozymes are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486088
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  • 10
    Electronic Resource
    Electronic Resource
    Genetics of sunflower alcohol dehydrogenase: Adh 2 ,nonlinkage to Adh 1 and Adh 1 early alleles (1974)
    Springer
    Biochemical genetics 12 (1974), S. 385-392 
    Details
    ISSN: 1573-4927
    Keywords: Helianthus annuus ; alcohol dehydrogenase ; isozymes ; genetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Alcohol dehydrogenase (ADH) isozymes in annual sunflowers (Helianthus annuus) are dimers whose subunits are produced by two genes, Adh 1 and Adh 2 .The codominant F and S alleles of Adh 1 produce the slower-migrating set of three isozymes. The faster-migrating set of three isozymes is controlled by Adh 2 , which also has at least two alleles, F and S. Hybridization experiments indicated that the Adh 2 alleles segregate in expected Mendelian fashion and that Adh 1 and Adh 2 are not linked. A third common 1-locus allele is designated early (E) because when homozygous it results in a blank at the 1FF isozyme position in mature seeds, but in developing seeds produces a normal-appearing band at the 1FF position. Hybridization studies showed that the early alleles segregated normally. Correlation between genotype and presence or absence of isozymes electrophoretically intermediate between those of Adh 1 and Adh 2 suggests that four intergenic isozymes may be formed as a result of dimerization of the four basic subunits. Studies of zymograms of developing seeds suggest that the remaining but inconstant zymogram bands are mature seed isozymes which have altered charges during early morphogenesis and thus are developmental artifacts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486643
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