Allozymes

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Patrick Berrebi - One of the best experts on this subject based on the ideXlab platform.

  • Natural and artificial secondary contact in brown trout (Salmo trutta, L.) in the French western Pyrenees assessed by Allozymes and microsatellites
    Heredity, 2002
    Co-Authors: D. Aurelle, G. Cattaneo-berrebi, Patrick Berrebi
    Abstract:

    Analysis of allozyme polymorphism in brown trout (Salmo trutta) populations from south-western France shows that two genetically differentiated wild forms (characterised by the LDH-C1*100 and 90 alleles) introgress in this area. As Allozymes could not evaluate the impact of stocking in the Atlantic basin, microsatellites have been necessary to detect the influence of hatchery fish and to confirm that the observed structure was natural. Microsatellites confirm the distinctness of the two wild forms based on allozyme loci. This situation provides a new example of secondary contact for this species in the Atlantic basin, with various levels of mixing being seen between the two population groups. The origin of these forms is discussed in the light of previous studies concerning modern and ancestral Atlantic trout (Hamilton et al, 1989) and lineages stemming from different glacial refuges (Garcia Marin et al, 1999; Weiss et al, 2000). This local analysis provides new insights in defining the evolutionary history of this species and confirms the important role of glaciation events in this history.

  • Biogeography and pattern of gene flow among Barbus species (Teleostei: Cyprinidae) inhabiting the Italian Peninsula and neighbouring Adriatic drainages as revealed by allozyme and mitochondrial sequence data
    Biological Journal of the Linnean Society, 2002
    Co-Authors: Costas S Tsigenopoulos, Petr Kotlik, Patrick Berrebi
    Abstract:

    Genetic relationships among 24 Italian and Adriatic populations of barbs (genus Barbus) were assessed using electrophoretic analysis of Allozymes and mitochondrial DNA sequences of the cytochrome b gene. Results obtained with both markers were concordant, but they were not congruent with the current morphology-based systematics and taxonomy. Populations assigned to the same nominal taxa (B. caninus, B. petenyi and B. rebeli), were very divergent in both Allozymes and mtDNA, indicating that these populations deserve recognition as different units for conservation and management. On the other hand, the two fluvio-lacustrine taxa considered as distinct species (i.e. B. plebejus and B. tyberinus) are genetically very close to each other, showing no clear differences at either Allozymes or mtDNA. The population of B. caninus from Pellice River carried allozyme alleles and mtDNA specific for B. plebejus, indicating a genetic introgression towards the former species.

  • biogeography and pattern of gene flow among barbus species teleostei cyprinidae inhabiting the italian peninsula and neighbouring adriatic drainages as revealed by allozyme and mitochondrial sequence data
    Biological Journal of The Linnean Society, 2002
    Co-Authors: Costas S Tsigenopoulos, Petr Kotlik, Patrick Berrebi
    Abstract:

    Genetic relationships among 24 Italian and Adriatic populations of barbs (genus Barbus) were assessed using electrophoretic analysis of Allozymes and mitochondrial DNA sequences of the cytochrome b gene. Results obtained with both markers were concordant, but they were not congruent with the current morphology-based systematics and taxonomy. Populations assigned to the same nominal taxa (B. caninus, B. petenyi and B. rebeli), were very divergent in both Allozymes and mtDNA, indicating that these populations deserve recognition as different units for conservation and management. On the other hand, the two fluvio-lacustrine taxa considered as distinct species (i.e. B. plebejus and B. tyberinus) are genetically very close to each other, showing no clear differences at either Allozymes or mtDNA. The population of B. caninus from Pellice River carried allozyme alleles and mtDNA specific for B. plebejus, indicating a genetic introgression towards the former species. © 2002 The Linnean Society of London, Biological Journal of the Linnean Society, 2002, 75, 83–99.

Yannis D. Clonis - One of the best experts on this subject based on the ideXlab platform.

  • isoenzyme and allozyme specific inhibitors 2 2 dihydroxybenzophenones and their carbonyl n analogues that discriminate between human glutathione transferase a1 1 and p1 1 Allozymes
    Chemical Biology & Drug Design, 2015
    Co-Authors: Foteini M Pouliou, Trias Thireou, Elias Eliopoulos, Petros G. Tsoungas, Nikolaos E. Labrou, Yannis D. Clonis
    Abstract:

    The selectivity of certain benzophenones and their carbonyl N-analogues was investigated towards the human GSTP1-1 Allozymes A, B and C involved in MDR. The Allozymes were purified from extracts derived from E. coli harbouring the plasmids pEXP5-CT/TOPO-TA-hGSTP1*A, pOXO4-hGSTP1*B or pOXO4-hGSTP1*C. Compound screening with each allozyme activity indicated three compounds with appreciable inhibitory potencies, 12 and 13 with P1-1A 62% and 67%, 11 and 12 with P1-1C 51% and 70%, whereas that of 15 fell behind with P1-1B (41%). These findings were confirmed by IC50 values (74-125 μm). Enzyme inhibition kinetics, aided by molecular modelling and docking, revealed that there is competition with the substrate CDNB for the same binding site on the allozyme (Ki(13/A)  = 63.6 ± 3.0 μm, Ki(15/B)  = 198.6 ± 14.3 μm, and Ki(11/C)  = 16.5 ± 2.7 μm). These data were brought into context by an in silico structural comparative analysis of the targeted proteins. Although the screened compounds showed moderate inhibitory potency against hGSTP1-1, remarkably, some of them demonstrated absolute isoenzyme and/or allozyme selectivity.

  • Isoenzyme‐ and Allozyme‐Specific Inhibitors: 2,2′‐Dihydroxybenzophenones and Their Carbonyl N‐Analogues that Discriminate between Human Glutathione Transferase A1‐1 and P1‐1 Allozymes
    Chemical biology & drug design, 2015
    Co-Authors: Foteini M Pouliou, Trias Thireou, Elias Eliopoulos, Petros G. Tsoungas, Nikolaos E. Labrou, Yannis D. Clonis
    Abstract:

    The selectivity of certain benzophenones and their carbonyl N-analogues was investigated towards the human GSTP1-1 Allozymes A, B and C involved in MDR. The Allozymes were purified from extracts derived from E. coli harbouring the plasmids pEXP5-CT/TOPO-TA-hGSTP1*A, pOXO4-hGSTP1*B or pOXO4-hGSTP1*C. Compound screening with each allozyme activity indicated three compounds with appreciable inhibitory potencies, 12 and 13 with P1-1A 62% and 67%, 11 and 12 with P1-1C 51% and 70%, whereas that of 15 fell behind with P1-1B (41%). These findings were confirmed by IC50 values (74-125 μm). Enzyme inhibition kinetics, aided by molecular modelling and docking, revealed that there is competition with the substrate CDNB for the same binding site on the allozyme (Ki(13/A)  = 63.6 ± 3.0 μm, Ki(15/B)  = 198.6 ± 14.3 μm, and Ki(11/C)  = 16.5 ± 2.7 μm). These data were brought into context by an in silico structural comparative analysis of the targeted proteins. Although the screened compounds showed moderate inhibitory potency against hGSTP1-1, remarkably, some of them demonstrated absolute isoenzyme and/or allozyme selectivity.

Costas S Tsigenopoulos - One of the best experts on this subject based on the ideXlab platform.

Foteini M Pouliou - One of the best experts on this subject based on the ideXlab platform.

  • isoenzyme and allozyme specific inhibitors 2 2 dihydroxybenzophenones and their carbonyl n analogues that discriminate between human glutathione transferase a1 1 and p1 1 Allozymes
    Chemical Biology & Drug Design, 2015
    Co-Authors: Foteini M Pouliou, Trias Thireou, Elias Eliopoulos, Petros G. Tsoungas, Nikolaos E. Labrou, Yannis D. Clonis
    Abstract:

    The selectivity of certain benzophenones and their carbonyl N-analogues was investigated towards the human GSTP1-1 Allozymes A, B and C involved in MDR. The Allozymes were purified from extracts derived from E. coli harbouring the plasmids pEXP5-CT/TOPO-TA-hGSTP1*A, pOXO4-hGSTP1*B or pOXO4-hGSTP1*C. Compound screening with each allozyme activity indicated three compounds with appreciable inhibitory potencies, 12 and 13 with P1-1A 62% and 67%, 11 and 12 with P1-1C 51% and 70%, whereas that of 15 fell behind with P1-1B (41%). These findings were confirmed by IC50 values (74-125 μm). Enzyme inhibition kinetics, aided by molecular modelling and docking, revealed that there is competition with the substrate CDNB for the same binding site on the allozyme (Ki(13/A)  = 63.6 ± 3.0 μm, Ki(15/B)  = 198.6 ± 14.3 μm, and Ki(11/C)  = 16.5 ± 2.7 μm). These data were brought into context by an in silico structural comparative analysis of the targeted proteins. Although the screened compounds showed moderate inhibitory potency against hGSTP1-1, remarkably, some of them demonstrated absolute isoenzyme and/or allozyme selectivity.

  • Isoenzyme‐ and Allozyme‐Specific Inhibitors: 2,2′‐Dihydroxybenzophenones and Their Carbonyl N‐Analogues that Discriminate between Human Glutathione Transferase A1‐1 and P1‐1 Allozymes
    Chemical biology & drug design, 2015
    Co-Authors: Foteini M Pouliou, Trias Thireou, Elias Eliopoulos, Petros G. Tsoungas, Nikolaos E. Labrou, Yannis D. Clonis
    Abstract:

    The selectivity of certain benzophenones and their carbonyl N-analogues was investigated towards the human GSTP1-1 Allozymes A, B and C involved in MDR. The Allozymes were purified from extracts derived from E. coli harbouring the plasmids pEXP5-CT/TOPO-TA-hGSTP1*A, pOXO4-hGSTP1*B or pOXO4-hGSTP1*C. Compound screening with each allozyme activity indicated three compounds with appreciable inhibitory potencies, 12 and 13 with P1-1A 62% and 67%, 11 and 12 with P1-1C 51% and 70%, whereas that of 15 fell behind with P1-1B (41%). These findings were confirmed by IC50 values (74-125 μm). Enzyme inhibition kinetics, aided by molecular modelling and docking, revealed that there is competition with the substrate CDNB for the same binding site on the allozyme (Ki(13/A)  = 63.6 ± 3.0 μm, Ki(15/B)  = 198.6 ± 14.3 μm, and Ki(11/C)  = 16.5 ± 2.7 μm). These data were brought into context by an in silico structural comparative analysis of the targeted proteins. Although the screened compounds showed moderate inhibitory potency against hGSTP1-1, remarkably, some of them demonstrated absolute isoenzyme and/or allozyme selectivity.

Petr Kotlik - One of the best experts on this subject based on the ideXlab platform.