Structural study of hemoglobin Hazebrouck, β38(C4)Thr → Pro A new abnormal hemoglobin with instability and low oxygen affinity

AbstractA new β-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 α-chains. The abnormal β-chain was readily separated from both βa- and αa-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 β38(C4)Thr → Pro was found, which was named Hb Hazebrouck