Enoki Y, Ohga Y, Furukawa K, Takaya A, Sakata S, Kohzuki H, Shimizu S, Tsujii T
Second Department of Physiology, Nara Medical University, Japan.
Hemoglobin. 1989;13(1):17-32. doi: 10.3109/03630268908998050.
A beta-variant hemoglobin, first misjudged as a marked elevation of Hb A1, was found in a 68-year-old Japanese female with diabetes mellitus. This hemoglobin was isolated by Bio-Rex 70 chromatography combined with chromatofocusing, and was found to be Hb Hope, beta 136(H14)Gly----Asp, by classical and high performance liquid chromatographic peptide mapping techniques. Intrinsic oxygen affinity of this hemoglobin was approximately one-third as compared with that of Hb A0. This property was still observed in the constituent beta subunits isolated. Effects of such allosteric effectors as H+ (at a fixed concentration of Cl-), anion (Cl-), 2,3-diphosphoglycerate and carbon dioxide were more or less depressed. Among others, a marked reduction in the carbamate effect should be noted in a structural interpretation of the functional modifications. Subunit cooperativity, on the contrary, was not different from that in Hb A0 (n = 2.8-2.9). Explanation of these altered functions were attempted on the basis of the altered structure. The reduced stability of Hb Hope is also described.
在一名68岁的日本糖尿病女性患者中发现了一种β-变异血红蛋白，最初被误诊为Hb A1显著升高。这种血红蛋白通过Bio-Rex 70色谱结合色谱聚焦法分离出来，并通过经典和高效液相色谱肽图谱技术鉴定为Hb Hope，β136(H14)Gly----Asp。这种血红蛋白的内在氧亲和力约为Hb A0的三分之一。在分离出的组成β亚基中仍观察到这种特性。H+(在固定Cl-浓度下)、阴离子(Cl-)、2,3-二磷酸甘油酸和二氧化碳等变构效应剂的作用或多或少受到抑制。其中，在对功能修饰的结构解释中应注意氨基甲酸盐效应的显著降低。相反，亚基协同性与Hb A0中的协同性没有差异(n = 2.8-2.9)。基于结构改变尝试对这些改变的功能进行解释。还描述了Hb Hope稳定性的降低。
