Blouquit Y, Delanoe-Garin J, Lacombe C, Arous N, Cayre Y, Peduzzi J, Braconnier F, Galacteros F
FEBS Lett. 1984 Jul 9;172(2):155-8. doi: 10.1016/0014-5793(84)81116-3.
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.
在一名有溶血性贫血终身病史的法国男性中检测到一种新的β变体，并对其进行了结构定义。该变体中度不稳定，氧亲和力低。标准电泳程序未检测到异常血红蛋白。在等电聚焦（IEF）过程中，它的移动速度比Hb A略慢。还观察到两个小部分；第一个迁移到Hb F的阴极，部分氧化的Hb A或一些不稳定血红蛋白的高铁血红蛋白衍生物也是如此；第二个在游离α链的位置。通过酸性尿素- Triton球蛋白链电泳，异常β链很容易与βA链和αA链分离。通过胰蛋白酶肽的指纹图谱和高效液相色谱（HPLC）同时进行结构研究。发现了一个新的突变β38（C4）Thr→Pro，命名为Hb Hazebrouck。
