Structural study of hemoglobin Hazebrouck, beta 38(C4)Thr----Pro. A new abnormal hemoglobin with instability and low oxygen affinity |
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Authors: | Y Blouquit J Delanoe-Garin C Lacombe N Arous Y Cayre J Peduzzi F Braconnier F Galacteros |
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Institution: | 1. Unité INSERM U-91, Hôpital Henri Mondor, 94010 CréteilFrance;2. Service d''Hématologie, Hôpital La PitiéSalpétrière, 75013 Paris, France |
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Abstract: | A new beta-variant has been detected and structurally defined in a French male, with a life-long history of hemolytic anemia. This variant is moderately unstable and has a low oxygen affinity. The abnormal hemoglobin was not detected by standard electrophoretic procedures. It moved slightly slower than Hb A during isoelectric focusing (IEF). Two minor fractions were also seen; the first migrated just cathodal to Hb F, as did partially oxidized Hb A or hemichrome derivatives of some unstable hemoglobins; the second in the position of free alpha-chains. The abnormal beta-chain was readily separated from both beta A- and alpha A-chains by acid-urea-Triton globin chain electrophoresis. Structural study was conducted simultaneously by fingerprinting and high-performance liquid chromatography (HPLC) of tryptic peptides. A new mutation beta 38(C4)Thr----Pro was found, which was named Hb Hazebrouck. |
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Keywords: | Hemoglobinopathy β-variant Molecular instability Low oxygen affinity HPLC Structural analysis |
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