The Experts below are selected from a list of 144 Experts worldwide ranked by ideXlab platform

F Galacteros - One of the best experts on this subject based on the ideXlab platform.

  • unstable alpha chain hemoglobin variants with factitious beta thalassemia biosynthetic ratio hb questembert α131 h14 ser pro and hb caen α132 h15 val gly
    American Journal of Hematology, 1993
    Co-Authors: H Wajcman, Corinne Vasseur, Y Blouquit, J Rosa, Dominique Labie, A Najman, O Reman, M Leporrier, F Galacteros
    Abstract:

    : Hb Questembert [alpha 131(H14)Ser-->Pro] was found in several members of a French family suffering from congenital Heinz Body Anemia. The unstable hemoglobin was expressed in the peripheral red blood cells at a very low level. Globin biosynthetic studies revealed a high specific activity of the abnormal chain and an alpha-/beta-labeling ratio similar to that of beta-thalassemia trait. Hb Caen [alpha 132(H15) Val-->Gly] is another unstable variant with the same globin biosynthesis abnormality. In both cases the structural modification is localized at the end of the H helix, a region encoded by the third exon. The mechanism for the unbalanced globin synthesis is not yet clear. It may be related 1) to a defect in chain assembly, 2) to an increased rate of degradation of the variant chain followed by the release of unlabeled beta-chains from the abnormal hemoglobin, thus leading to an apparent suppression of beta-chain synthesis, or 3) to a modified stability of the abnormal alpha-globin mRNA.

H Wajcman - One of the best experts on this subject based on the ideXlab platform.

  • unstable alpha chain hemoglobin variants with factitious beta thalassemia biosynthetic ratio hb questembert α131 h14 ser pro and hb caen α132 h15 val gly
    American Journal of Hematology, 1993
    Co-Authors: H Wajcman, Corinne Vasseur, Y Blouquit, J Rosa, Dominique Labie, A Najman, O Reman, M Leporrier, F Galacteros
    Abstract:

    : Hb Questembert [alpha 131(H14)Ser-->Pro] was found in several members of a French family suffering from congenital Heinz Body Anemia. The unstable hemoglobin was expressed in the peripheral red blood cells at a very low level. Globin biosynthetic studies revealed a high specific activity of the abnormal chain and an alpha-/beta-labeling ratio similar to that of beta-thalassemia trait. Hb Caen [alpha 132(H15) Val-->Gly] is another unstable variant with the same globin biosynthesis abnormality. In both cases the structural modification is localized at the end of the H helix, a region encoded by the third exon. The mechanism for the unbalanced globin synthesis is not yet clear. It may be related 1) to a defect in chain assembly, 2) to an increased rate of degradation of the variant chain followed by the release of unlabeled beta-chains from the abnormal hemoglobin, thus leading to an apparent suppression of beta-chain synthesis, or 3) to a modified stability of the abnormal alpha-globin mRNA.

  • Unstable alpha‐chain hemoglobin variants with factitious beta‐thalassemia biosynthetic ratio: Hb questembert (α131[H14] Ser→Pro) and Hb Caen (α132[H15] Val→Gly)
    American Journal of Hematology, 1993
    Co-Authors: H Wajcman, Yves Blouquit, Jean-philippe Rosa, Corinne Vasseur, Dominique Labie, O Reman, M Leporrier, Najman A, Frédéric Galactéros
    Abstract:

    Hb Questembert [alpha 131(H14)Ser-->Pro] was found in several members of a French family suffering from congenital Heinz Body Anemia. The unstable hemoglobin was expressed in the peripheral red blood cells at a very low level. Globin biosynthetic studies revealed a high specific activity of the abnormal chain and an alpha-/beta-labeling ratio similar to that of beta-thalassemia trait. Hb Caen [alpha 132(H15) Val-->Gly] is another unstable variant with the same globin biosynthesis abnormality. In both cases the structural modification is localized at the end of the H helix, a region encoded by the third exon. The mechanism for the unbalanced globin synthesis is not yet clear. It may be related 1) to a defect in chain assembly, 2) to an increased rate of degradation of the variant chain followed by the release of unlabeled beta-chains from the abnormal hemoglobin, thus leading to an apparent suppression of beta-chain synthesis, or 3) to a modified stability of the abnormal alpha-globin mRNA.

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

  • unstable alpha chain hemoglobin variants with factitious beta thalassemia biosynthetic ratio hb questembert α131 h14 ser pro and hb caen α132 h15 val gly
    American Journal of Hematology, 1993
    Co-Authors: H Wajcman, Corinne Vasseur, Y Blouquit, J Rosa, Dominique Labie, A Najman, O Reman, M Leporrier, F Galacteros
    Abstract:

    : Hb Questembert [alpha 131(H14)Ser-->Pro] was found in several members of a French family suffering from congenital Heinz Body Anemia. The unstable hemoglobin was expressed in the peripheral red blood cells at a very low level. Globin biosynthetic studies revealed a high specific activity of the abnormal chain and an alpha-/beta-labeling ratio similar to that of beta-thalassemia trait. Hb Caen [alpha 132(H15) Val-->Gly] is another unstable variant with the same globin biosynthesis abnormality. In both cases the structural modification is localized at the end of the H helix, a region encoded by the third exon. The mechanism for the unbalanced globin synthesis is not yet clear. It may be related 1) to a defect in chain assembly, 2) to an increased rate of degradation of the variant chain followed by the release of unlabeled beta-chains from the abnormal hemoglobin, thus leading to an apparent suppression of beta-chain synthesis, or 3) to a modified stability of the abnormal alpha-globin mRNA.

  • Unstable alpha‐chain hemoglobin variants with factitious beta‐thalassemia biosynthetic ratio: Hb questembert (α131[H14] Ser→Pro) and Hb Caen (α132[H15] Val→Gly)
    American Journal of Hematology, 1993
    Co-Authors: H Wajcman, Yves Blouquit, Jean-philippe Rosa, Corinne Vasseur, Dominique Labie, O Reman, M Leporrier, Najman A, Frédéric Galactéros
    Abstract:

    Hb Questembert [alpha 131(H14)Ser-->Pro] was found in several members of a French family suffering from congenital Heinz Body Anemia. The unstable hemoglobin was expressed in the peripheral red blood cells at a very low level. Globin biosynthetic studies revealed a high specific activity of the abnormal chain and an alpha-/beta-labeling ratio similar to that of beta-thalassemia trait. Hb Caen [alpha 132(H15) Val-->Gly] is another unstable variant with the same globin biosynthesis abnormality. In both cases the structural modification is localized at the end of the H helix, a region encoded by the third exon. The mechanism for the unbalanced globin synthesis is not yet clear. It may be related 1) to a defect in chain assembly, 2) to an increased rate of degradation of the variant chain followed by the release of unlabeled beta-chains from the abnormal hemoglobin, thus leading to an apparent suppression of beta-chain synthesis, or 3) to a modified stability of the abnormal alpha-globin mRNA.

O Reman - One of the best experts on this subject based on the ideXlab platform.

  • unstable alpha chain hemoglobin variants with factitious beta thalassemia biosynthetic ratio hb questembert α131 h14 ser pro and hb caen α132 h15 val gly
    American Journal of Hematology, 1993
    Co-Authors: H Wajcman, Corinne Vasseur, Y Blouquit, J Rosa, Dominique Labie, A Najman, O Reman, M Leporrier, F Galacteros
    Abstract:

    : Hb Questembert [alpha 131(H14)Ser-->Pro] was found in several members of a French family suffering from congenital Heinz Body Anemia. The unstable hemoglobin was expressed in the peripheral red blood cells at a very low level. Globin biosynthetic studies revealed a high specific activity of the abnormal chain and an alpha-/beta-labeling ratio similar to that of beta-thalassemia trait. Hb Caen [alpha 132(H15) Val-->Gly] is another unstable variant with the same globin biosynthesis abnormality. In both cases the structural modification is localized at the end of the H helix, a region encoded by the third exon. The mechanism for the unbalanced globin synthesis is not yet clear. It may be related 1) to a defect in chain assembly, 2) to an increased rate of degradation of the variant chain followed by the release of unlabeled beta-chains from the abnormal hemoglobin, thus leading to an apparent suppression of beta-chain synthesis, or 3) to a modified stability of the abnormal alpha-globin mRNA.

  • Unstable alpha‐chain hemoglobin variants with factitious beta‐thalassemia biosynthetic ratio: Hb questembert (α131[H14] Ser→Pro) and Hb Caen (α132[H15] Val→Gly)
    American Journal of Hematology, 1993
    Co-Authors: H Wajcman, Yves Blouquit, Jean-philippe Rosa, Corinne Vasseur, Dominique Labie, O Reman, M Leporrier, Najman A, Frédéric Galactéros
    Abstract:

    Hb Questembert [alpha 131(H14)Ser-->Pro] was found in several members of a French family suffering from congenital Heinz Body Anemia. The unstable hemoglobin was expressed in the peripheral red blood cells at a very low level. Globin biosynthetic studies revealed a high specific activity of the abnormal chain and an alpha-/beta-labeling ratio similar to that of beta-thalassemia trait. Hb Caen [alpha 132(H15) Val-->Gly] is another unstable variant with the same globin biosynthesis abnormality. In both cases the structural modification is localized at the end of the H helix, a region encoded by the third exon. The mechanism for the unbalanced globin synthesis is not yet clear. It may be related 1) to a defect in chain assembly, 2) to an increased rate of degradation of the variant chain followed by the release of unlabeled beta-chains from the abnormal hemoglobin, thus leading to an apparent suppression of beta-chain synthesis, or 3) to a modified stability of the abnormal alpha-globin mRNA.

Dominique Labie - One of the best experts on this subject based on the ideXlab platform.

  • unstable alpha chain hemoglobin variants with factitious beta thalassemia biosynthetic ratio hb questembert α131 h14 ser pro and hb caen α132 h15 val gly
    American Journal of Hematology, 1993
    Co-Authors: H Wajcman, Corinne Vasseur, Y Blouquit, J Rosa, Dominique Labie, A Najman, O Reman, M Leporrier, F Galacteros
    Abstract:

    : Hb Questembert [alpha 131(H14)Ser-->Pro] was found in several members of a French family suffering from congenital Heinz Body Anemia. The unstable hemoglobin was expressed in the peripheral red blood cells at a very low level. Globin biosynthetic studies revealed a high specific activity of the abnormal chain and an alpha-/beta-labeling ratio similar to that of beta-thalassemia trait. Hb Caen [alpha 132(H15) Val-->Gly] is another unstable variant with the same globin biosynthesis abnormality. In both cases the structural modification is localized at the end of the H helix, a region encoded by the third exon. The mechanism for the unbalanced globin synthesis is not yet clear. It may be related 1) to a defect in chain assembly, 2) to an increased rate of degradation of the variant chain followed by the release of unlabeled beta-chains from the abnormal hemoglobin, thus leading to an apparent suppression of beta-chain synthesis, or 3) to a modified stability of the abnormal alpha-globin mRNA.

  • Unstable alpha‐chain hemoglobin variants with factitious beta‐thalassemia biosynthetic ratio: Hb questembert (α131[H14] Ser→Pro) and Hb Caen (α132[H15] Val→Gly)
    American Journal of Hematology, 1993
    Co-Authors: H Wajcman, Yves Blouquit, Jean-philippe Rosa, Corinne Vasseur, Dominique Labie, O Reman, M Leporrier, Najman A, Frédéric Galactéros
    Abstract:

    Hb Questembert [alpha 131(H14)Ser-->Pro] was found in several members of a French family suffering from congenital Heinz Body Anemia. The unstable hemoglobin was expressed in the peripheral red blood cells at a very low level. Globin biosynthetic studies revealed a high specific activity of the abnormal chain and an alpha-/beta-labeling ratio similar to that of beta-thalassemia trait. Hb Caen [alpha 132(H15) Val-->Gly] is another unstable variant with the same globin biosynthesis abnormality. In both cases the structural modification is localized at the end of the H helix, a region encoded by the third exon. The mechanism for the unbalanced globin synthesis is not yet clear. It may be related 1) to a defect in chain assembly, 2) to an increased rate of degradation of the variant chain followed by the release of unlabeled beta-chains from the abnormal hemoglobin, thus leading to an apparent suppression of beta-chain synthesis, or 3) to a modified stability of the abnormal alpha-globin mRNA.