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  • 1
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— We have studied the dynamics of the appearance of cells reacting positively with anti-S-100 protein antiserum, during postnatal neurocytogenesis in the brain of rats of two strains differing in their susceptibility to sound stimuli. The postnatal time of appearance of cells reacting positively with anti-S-100 protein antiserum was somewhat later in rats susceptible to sound-induced seizures than in sound-resistant rats. These differences concerned mainly the cerebral cortex of 12-day-old rats. By day 21 of postnatal life these differences had disappeared. In subcortical structures of the brain, S-100 protein was first found on the 4th to the 5th day of life and the rate of appearance of cells containing this protein was similar in the two strains.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 39 (1983), S. 878-880 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary It is shown that the potent protease inhibitor phenylmethylsulphonylfluoride (PMSF) strongly inhibits the activity of allDrosophila esterases but β-esterase. We suggest the application of PMSF for the selective staining of β-esterase inDrosophila tissues.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-4927
    Keywords: esterases ; Drosophila virilis ; electrophoresis ; Drosophila embryogenesis ; gene activation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Changes in esterase patterns in hybrids between Drosophila virilis stocks differing in the electrophoretic mobilities of certain esterase fractions have been studied by means of starch and polyacrylamide gel electrophoresis. It has been established that parental esterases are expressed synchronously during the period of the end of embryogenesis to the beginning of first instar larvae. This period coincides with the biochemically detected increase in esterase activity.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-4927
    Keywords: esterases ; Drosophila virilis ; electrophoresis ; heat sensitivity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract From analysis of the properties of the “pupal” esterase (p-esterase) in Drosophila virilis, it is concluded that it is heat stable, its electrophoretic detection depends on culture density, its expression is stage specific, and it is not a variant of esterase 2. It was also demonstrated that p-esterase, like esterase 6, is activated by injections of the juvenile hormone into larvae. Heat treatment of heat-resistant D. virilis stocks led to decreased activities of the juvenile hormone dependent esterases but did not affect those of the heat-sensitive stocks. It is suggested that heat resistance in D. virilis is related to some functional features of the system of modifier genes controlling the phenotypic expression of esterases.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-4927
    Keywords: esterases ; Drosophila imeretensis ; electrophoresis ; interspecific hybrids ; gene activation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A slow-migrating β-esterase (S-esterase) is described which has been detected in Drosophila montana, Drosophila imeretensis, and some stocks of Drosophila virilis when mixtures of α- and β-naphthyl acetate are used as substrates in histochemical reactions after electrophoresis. Sexual dimorphism for S-esterase has been demonstrated. This esterase is contained in male genitalia only, predominantly in the ejaculatory bulb (waxy plug). It appears 3–4 days after emergence of flies. In hybrids between S+ and S0 species, the activity of the slow esterase is either decreased or inhibited. An autonomous synthesis of the S-esterase in the ejaculatory bulb was established by transplantation of imaginal genital discs into larvae of different Drosophila stocks. Based on analysis of physicochemical and immunochemical properties, S-esterase is suggested to be an independent fraction of esterase, possibly dimeric, which does not cross-react with β-esterase antiserum.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1573-4927
    Keywords: esterase ; Drosophila virilis ; juvenile hormone ; electrophoresis ; heat sensitivity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The heat-resistant subline 147S was obtained in Drosophila virilis by selecting for viability individuals of heat-sensitive stock 147. It was shown that in the heat-treated 147S pupae the activity of juvenile hormone (JH)-esterase is decreased and, consequently, the titer of juvenile hormone is increased compared with those in the control pupae. These changes are consistent with those observed earlier for resistant stock 101. Heat-resistant stocks 101 and 147S were crossed with heat-sensitive stock 147, whose heat-treated larvae show earlier activation and higher activity of JH-esterase than control larvae. The viability and electrophoretic esterase patterns were analyzed in the F1 and F2 hybrids at different temperatures. It was found that the F1 hybrid is resistant to the effect of high temperature and its activity level of JH-esterase is lower compared with controls. In the F2 hybrid, there was a 3:1 segregation of viability and a 1:2:1 segregation of the activity level of JH-esterase at high temperatures. It is concluded that the activity level of JH-esterase and heat resistance in D. virilis are monogenically controlled at high temperatures.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1573-4927
    Keywords: JH-esterase ; Drosophila virilis ; extreme conditions ; electrophoresis ; radial immunodiffusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The content of JH-esterase was assayed by radial immunodiffusion in Drosophila virilis pupae under normal conditions and under the effects of extreme factors. It was found that JH-esterase content is the same (not different from the control) in pupae showing a high activity of the enzyme and in those not showing it. These data are evidence for a gene controlling JH-esterase activity. It was also shown that a regulatory factor converts inactive into active JH-esterase when homogenates of pupae, with active and inactive forms, were mixed and incubated together. It was demonstrated that the source of the activating factor is the larval brain. Sublines 147-R and 147-I were produced by introducing the second chromosome pair of stocks 103 and 101, which are heat resistant, into the genome of individuals of stock 147, which is heat sensitive. Sublines 160-III, 160-IV, 160-V, and 160-VI were produced by introducing the third, fourth, fifth, and sixth chromosome pairs of stock 147 into the genome of stock 160S, which is heat-resistant. The results of analysis of JH-esterase activity and the viability of individuals of these sublines at high temperatures indicated that the gene regulating the activity of JH-esterase is located in the sixth chromosome of D. virilis.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1573-4927
    Keywords: genetics ; electrophoresis ; biochemical polymorphism ; Drosophila littoralis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract We have investigated 13 alleles of four genes coding for acid phosphatase, α-and β-esterases, and malic enzyme. The genes were localized and their positions regarding the centromere are as follows: Acph-1—centromere—Me—cu—dt—α-Est—[Inversion 2t]—β-Est. The occurrence of crossing-over in Drosophila imeretensis males, as well as the tetrameric structure of malic enzyme, was confirmed.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1573-4927
    Keywords: Drosophila virilis ; juvenile hormone (JH) ; JH-esterase ; ontogenesis ; high temperatures
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The kinetic characteristics of the main isozymes ofDrosophila virilis esterase were studied andK m values of esterase-2, -4, and -6 and p-esterase for α- and β-naphthyl acetate were obtained. Juvenile hormone (JH) was shown to inhibit the p-esterase activity when in competition with β-naphthyl acetate and the general esterase inhibitor, diisopropylphosphofluoridate (DFP), was shown to inhibit all the components of theD. virilis esterase patterns except p-esterase. While studying the changes of p-esterase activity inD. virilis ontogenesis, the increase in p-esterase activity in the wandering larvae, prepupae, and early pupae was found to correlate with a decrease in JH titer at these stages. The decrease in JH level in a temperature-sensitive lethal mutant larvae ofD. virilis at high temperatures was shown to correlate with increased p-esterase activity. These results confirm that p-esterease ofD. virilis is JH-esterase.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1573-4927
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Female rats of the Wistar strain were killed by decapitation in the stages of estrus and diestrus. RNA content was measured, and its base composition was determined by the microelectrophoresis method of Edström in neurosecretory cells of N. supraopticus of the hypothalamus. Cells were isolated from Carnoy-fixed tissue. Each sample consisted of 10–15 isolated cells. Significant differences between the average RNA content per nerve cell in estrus and diestrus were not observed (in estrus it was equal to 70.3±5.52 and in diestrus 88.4±9.14 picograms per cell). The adenine/uracil ratio was higher in diestrous stage than in estrus (1.35±0.16 and 0.88±0.05).
    Type of Medium: Electronic Resource
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