The Experts below are selected from a list of 21 Experts worldwide ranked by ideXlab platform

Nathalie Griffon - One of the best experts on this subject based on the ideXlab platform.

  • Globin and Globin Gene Structure of the Nerve MyoGlobin of Aphrodite aculeata
    The Journal of biological chemistry, 1996
    Co-Authors: Mark Blaxter, Michael C Marden, Jacques R Vanfleteren, Marie-louise Van Hauwaert, Eddy L. Esmans, Nathalie Griffon
    Abstract:

    Abstract The Globin of the nerve cord of the polychaete annelid Aphrodite aculeata was isolated and purified to homogeneity. The native molecule has a pI of 6.3 and acts as a dimer of two identical Mr 15,644.5 polypeptide chains as determined by electrospray mass spectrometry. It has an average affinity for oxygen (P50 = 1.24 torr) resulting from fast association (kon = 170 × 106 M−1·s−1) and dissociation rates (koff = 360 s−1). The partial primary structure of this nerve Globin was determined at the protein level and completed and confirmed by translation of the cDNA sequence. The Globin chain has 150 amino acid residues and a calculated Mr of 15,602.69 strongly suggesting that the amino terminus is acetylated. The absence of a leader sequence and the lack of Cys at the positions NA2 and H9 needed for the formation of the high Mr complexes found in extracellular annelid Globins classify the Aphrodite Globin with the cellular Globin species. The Aphrodite nerve Globin is unlikely to represent a separate Globin family, as cDNA derived primers detect Globin Messenger RNA in muscle, gut, and pharynx tissue as well. The gene encoding this Globin species is interrupted by a single intron, inserted at position G7.0. Comparison to other Globin gene structures strongly suggest that introns can be lost independently, rather than simultaneously as a result of a single conversion event as suggested previously (Lewin, R. (1984) Science 226, 328).

Mark Blaxter - One of the best experts on this subject based on the ideXlab platform.

  • Globin and Globin Gene Structure of the Nerve MyoGlobin of Aphrodite aculeata
    The Journal of biological chemistry, 1996
    Co-Authors: Mark Blaxter, Michael C Marden, Jacques R Vanfleteren, Marie-louise Van Hauwaert, Eddy L. Esmans, Nathalie Griffon
    Abstract:

    Abstract The Globin of the nerve cord of the polychaete annelid Aphrodite aculeata was isolated and purified to homogeneity. The native molecule has a pI of 6.3 and acts as a dimer of two identical Mr 15,644.5 polypeptide chains as determined by electrospray mass spectrometry. It has an average affinity for oxygen (P50 = 1.24 torr) resulting from fast association (kon = 170 × 106 M−1·s−1) and dissociation rates (koff = 360 s−1). The partial primary structure of this nerve Globin was determined at the protein level and completed and confirmed by translation of the cDNA sequence. The Globin chain has 150 amino acid residues and a calculated Mr of 15,602.69 strongly suggesting that the amino terminus is acetylated. The absence of a leader sequence and the lack of Cys at the positions NA2 and H9 needed for the formation of the high Mr complexes found in extracellular annelid Globins classify the Aphrodite Globin with the cellular Globin species. The Aphrodite nerve Globin is unlikely to represent a separate Globin family, as cDNA derived primers detect Globin Messenger RNA in muscle, gut, and pharynx tissue as well. The gene encoding this Globin species is interrupted by a single intron, inserted at position G7.0. Comparison to other Globin gene structures strongly suggest that introns can be lost independently, rather than simultaneously as a result of a single conversion event as suggested previously (Lewin, R. (1984) Science 226, 328).

Donald Lavelle - One of the best experts on this subject based on the ideXlab platform.

  • decitabine increases fetal hemoGlobin in papio anubis by increasing γ Globin gene transcription
    Experimental Hematology, 2010
    Co-Authors: Imo Akpan, Virryan Banzon, Vinzon Ibanez, Kestis Vaitkus, Joseph Desimone, Donald Lavelle
    Abstract:

    Objective The mechanism responsible for increased fetal hemoGlobin levels following decitabine treatment remains controversial. These experiments were performed to evaluate the role of transcriptional vs. translational mechanisms in the ability of decitabine to increase fetal hemoGlobin levels in vivo. Materials and Methods Three normal, nonanemic baboons were treated with decitabine subcutaneously (0.5 mg/kg/d) for 10 days. The effect of decitabine on Globin chain synthesis and Globin Messenger RNA levels was measured in pre- and posttreatment bone marrow aspirates by biosynthetic radiolabeling with [ 3 H] leucine followed by separation of Globin chains by high-performance liquid chromatography, and real-time polymerase chain reaction, respectively. The effect on DNA methylation of the ɛ- and γ-Globin gene promoters was determined by bisulfite sequence analysis. Results Decitabine treatment of normal, nonanemic baboons induced similar increases in the γ/γ+β chain synthetic ratio and the γ/total β-like Globin RNA ratio and also increased expression of ɛ-Globin transcripts. Increased expression of ɛ- and γ-Globin was associated with decreased DNA methylation of the ɛ- and γ-Globin gene promoters. Conclusions Decitabine increases fetal hemoGlobin in vivo by transcriptional activation of the γ-Globin gene.

Jacques R Vanfleteren - One of the best experts on this subject based on the ideXlab platform.

  • Globin and Globin Gene Structure of the Nerve MyoGlobin of Aphrodite aculeata
    The Journal of biological chemistry, 1996
    Co-Authors: Mark Blaxter, Michael C Marden, Jacques R Vanfleteren, Marie-louise Van Hauwaert, Eddy L. Esmans, Nathalie Griffon
    Abstract:

    Abstract The Globin of the nerve cord of the polychaete annelid Aphrodite aculeata was isolated and purified to homogeneity. The native molecule has a pI of 6.3 and acts as a dimer of two identical Mr 15,644.5 polypeptide chains as determined by electrospray mass spectrometry. It has an average affinity for oxygen (P50 = 1.24 torr) resulting from fast association (kon = 170 × 106 M−1·s−1) and dissociation rates (koff = 360 s−1). The partial primary structure of this nerve Globin was determined at the protein level and completed and confirmed by translation of the cDNA sequence. The Globin chain has 150 amino acid residues and a calculated Mr of 15,602.69 strongly suggesting that the amino terminus is acetylated. The absence of a leader sequence and the lack of Cys at the positions NA2 and H9 needed for the formation of the high Mr complexes found in extracellular annelid Globins classify the Aphrodite Globin with the cellular Globin species. The Aphrodite nerve Globin is unlikely to represent a separate Globin family, as cDNA derived primers detect Globin Messenger RNA in muscle, gut, and pharynx tissue as well. The gene encoding this Globin species is interrupted by a single intron, inserted at position G7.0. Comparison to other Globin gene structures strongly suggest that introns can be lost independently, rather than simultaneously as a result of a single conversion event as suggested previously (Lewin, R. (1984) Science 226, 328).

Michael C Marden - One of the best experts on this subject based on the ideXlab platform.

  • Globin and Globin Gene Structure of the Nerve MyoGlobin of Aphrodite aculeata
    The Journal of biological chemistry, 1996
    Co-Authors: Mark Blaxter, Michael C Marden, Jacques R Vanfleteren, Marie-louise Van Hauwaert, Eddy L. Esmans, Nathalie Griffon
    Abstract:

    Abstract The Globin of the nerve cord of the polychaete annelid Aphrodite aculeata was isolated and purified to homogeneity. The native molecule has a pI of 6.3 and acts as a dimer of two identical Mr 15,644.5 polypeptide chains as determined by electrospray mass spectrometry. It has an average affinity for oxygen (P50 = 1.24 torr) resulting from fast association (kon = 170 × 106 M−1·s−1) and dissociation rates (koff = 360 s−1). The partial primary structure of this nerve Globin was determined at the protein level and completed and confirmed by translation of the cDNA sequence. The Globin chain has 150 amino acid residues and a calculated Mr of 15,602.69 strongly suggesting that the amino terminus is acetylated. The absence of a leader sequence and the lack of Cys at the positions NA2 and H9 needed for the formation of the high Mr complexes found in extracellular annelid Globins classify the Aphrodite Globin with the cellular Globin species. The Aphrodite nerve Globin is unlikely to represent a separate Globin family, as cDNA derived primers detect Globin Messenger RNA in muscle, gut, and pharynx tissue as well. The gene encoding this Globin species is interrupted by a single intron, inserted at position G7.0. Comparison to other Globin gene structures strongly suggest that introns can be lost independently, rather than simultaneously as a result of a single conversion event as suggested previously (Lewin, R. (1984) Science 226, 328).