The degree of polymorphisms in enzymes involved in energy production compared to that in nonspecific enzymes in two Drosophila ananassae populations.

Gillespie, John H.; Kojima, Ken-ichi

doi:10.1073/pnas.61.2.582

Cited by 188 publications

(81 citation statements)

References 6 publications

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“…These have been discussed in considerable detail by a number of authors including Hubby (1963), Hubby andThrockmorton (1965, 1968), Lewontin and Hubby (1966), Johnson et at. (1966) and Gillespie and Kojima (1968) and need not be reiterated here. It is sufficient to note that, at the present time, we cannot say whether we are underestimating or overestimating the cotal variation in the genome, or to what degree, if any, our estimates are biased.…”

Section: Discussomentioning

confidence: 99%

Isozyme polymorphisms in natural populations of Avena fatua and A. barbata

1970

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Section: Discussomentioning

confidence: 99%

Isozyme polymorphisms in natural populations of Avena fatua and A. barbata

1970

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“…Four of the most variable loci in deer are tetramers (f3Hb, aHb, Mod-2, and Sordh; table 1). Whitetails also do not show the predicted differences between functional groups of proteins (Gillespie and Kojima, 1968; The frequency distributions of loci with various numbers of alleles or h values also were significantly different between mammals in general and white-tailed deer (figs 1 and 2). The exact cause of the differences between white-tailed deer and mammals in general is not known, but they may be discovered through studies of the specific properties of the enzymes involved or through a better understanding of the population dynamics of white-tailed deer (Scribner et a!., 1985).…”

Section: Srpmentioning

confidence: 84%

“…group II = multi-substrate enzymes; group III = nonenzymatic proteins; Gillespie and Kojima, 1968). Mean H and A values were calculated for SRP and overall white-tailed deer, and one-way analyses of variance were calculated using an arcsin-square-root transformation of h values and a square-root transformation of A values.…”

Section: Methodsmentioning

confidence: 99%

Genetic variability in white-tailed deer

et al. 1988

Heredity

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Genetic variability at 36 loci was studied in white-tailed deer (Odocoileus virginianus) populations, on the Savannah River Plant (SRP) in South Carolina. Mean multilocus heterozygosity (H), percentage of polymorphic loci (P) and average number of alleles per locus (A) for white-tailed deer were calculated and compared with values for white-tailed deer from several locations (SRP deer: H =99 per cent, P005 = 30.6 per cent, A = 1 89; white-tailed deer overall: H = 10•4 per cent, P0.05 = 32.3 per cent, A = 1.94). Frequency distributions for single locus heterozygosity values (h) and the number of alleles per locus for white-tailed deer were found to be significantly different from those of mammals in general. Analysis of single-locus data based on quaternary structure and functional groups of proteins failed to demonstrate expected differences as predicted from the literature. White-tailed deer have a high level of heterozygosity, but they do not exhibit many of the life history and environmental characteristics associated with high heterozygosity in other animals.

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“…Transaldolase, an essen-tial enzyme in the "fructose 6-phosphate shunt," is characteristic of bifidobacteria because it acts upon fructose 6-phosphate and erythrose 4-phosphate after the initial formation of the latter from the former by a phosphoketolase; GPGD is apparently a functionless enzyme, at least in glucose-grown cells, which, as a rule, lack detectable glucose 6-phosphate dehydrogenase (4, 25). Different extents of variability in the two enzymes can reasonably be expected during the course of bifidobacterial evolution (e.g., see Gillespie and Kojima [6]). A preliminary immunological study on the structural relatedness of bifido bacterial transaldolases has recently been performed with the ultimate goal of elucidating the evolutionary relationships of these organisms (34).…”

Section: Fructosementioning

confidence: 99%

Multiple Electrophoretic Forms of Transaldolase and 6-Phosphogluconic Dehydrogenase and Their Relationships to the Taxonomy and Ecology of the Bifidobacteria

Scardovi

Casalicchio

Vincenzi

1979

International Journal of Systematic Bacteriology

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The electrophoretic patterns of the transaldolases and 6-phosphogluconate dehydrogenases (GPGD) of 1,206 strains, each belonging to one of 24 named species of the genus Bifidobacterium, were determined by means of starch-gel electrophoresis. All of these strains were previously assigned to species on the basis of their deoxyribonucleic acid homology relationships and were selected so as to include all known phenotypes and habitats. Fourteen electrophoretic forms of transaldolase and 19 of nicotinamide adenine dinucleotide phosphate-dependent GPGD were identified and numbered. Each strain displayed one band for each enzyme. Glucose-grown cells of the B. pullorum strains and of most of the B. dentium strains were devoid of detectable levels of GPGD. The zymograms of more than 60% of the strains studied were species specific. Nearly half of the other strains had significant overlapping of transaldolase and GPGD patterns, and they were assigned therefore to species on the basis of an additional marker, 3-phosphoglyceraldehyde dehydrogenase production, the results of which are not reported here in detail. Of the species studied, B. asteroides exhibited the greatest variability in electrophoretic types of both transaldolase and GPGD. Correlations between electrophoretic data, deoxyribonucleic acid homology relationships between the species, and ecology are discussed.Fructose 6-phosphate phosphoketolase (FGPPK) is the key enzyme of carbohydrate dissimilation in the genus Bifidobacterium. Although its relative electrophoretic mobility is generally not a useful character for species differentiation, there are some differences in the properties of F6PPK in some Bifodobacterium species generally confined to specific habitats. The most anodic form of F6PPK was from B. asteroides (from the honey bee intestine); a second, less mobile FGPPK was from B. globosum, B. thermophilum, and B. suis (commonly isolated from the feces of various animals); a third F6PPK isozyme of intermediate electrophoretic mobility was present in B. breve, B. longum, and B. adolescentis (human strains from intestine, dental caries, and vagina) (24). A comparative study of the FGPPKs from the type strains of B. globosum and B. dentium disclosed that the enzyme from B. globosum was more heat stable than that from B. dentium, that the optimum activity was at pH 5 to 6 for B. globosum and at pH 7 for B. dentium, and that the "animal" type of FGPPK (from B. globosum) was activated by Mg'+ and was less active in the presence of Mn2+, whereas the reverse was true with the "human" type of FGPPK (from B. dentium), where only Mn2+ fully activated the enzyme. The molecular weights were different (1.6 x lo5 and 2.9 X lo5, respectively), and the enzyme from B. globosum also cleaved xylulose 5-phosphate, whereas the B. dentium FGPPK was specific for fructose 6-phosphate (33).A preliminary study on the electrophoretic forms of other enzymes, such as transaldolase, transketolase, 6-phosphogluconate dehydrogenase (GPGD), and aldolase, was made with 49 representative st...

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The degree of polymorphisms in enzymes involved in energy production compared to that in nonspecific enzymes in two Drosophila ananassae populations.

Cited by 188 publications

References 6 publications

Isozyme polymorphisms in natural populations of Avena fatua and A. barbata

Isozyme polymorphisms in natural populations of Avena fatua and A. barbata

Genetic variability in white-tailed deer

Multiple Electrophoretic Forms of Transaldolase and 6-Phosphogluconic Dehydrogenase and Their Relationships to the Taxonomy and Ecology of the Bifidobacteria

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