Structural study of hemoglobin Hazebrouck, β38(C4)Thr → Pro

A 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.