Structural study of hemoglobin Hazebrouck, beta 38(C4)Thr----Pro. A new abnormal hemoglobin with instability and low oxygen affinity.
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.
D000328:Adult; D000596:Amino Acids / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D004586:Electrophoresis; D005914:Globins / Q000032:analysis; D006455:Hemoglobins, Abnormal / Q000032:analysis* / Q000302:isolation & purification; D006801:Humans; D007525:Isoelectric Focusing; D008297:Male; D010100:Oxygen / Q000097:blood; D011392:Proline / Q000032:analysis; D013912:Threonine / Q000032:analysis; D014357:Trypsin
D000596:Amino Acids; D006455:Hemoglobins, Abnormal; D013912:Threonine; D005914:Globins; C042224:hemoglobin Hazebrouck; D011392:Proline; D014357:Trypsin; D010100:Oxygen