Shapiro R, McManus M, Garrick L, McDonald M J, Bunn H F
Metabolism. 1979 Apr;28(4 Suppl 1):427-30. doi: 10.1016/0026-0495(79)90050-7.
The most abundant minor hemoglobin component of human hemolysate is Hb A1c, which has glucose bound to the N-terminus of the beta chain by a ketoamine linkage. Hb A1c is formed slowly and continuously throughout the 120 day lifespan of the red cell. It can be synthesized in vitro by incubating purified hemoglobin with 14C-glucose. Other minor components, Hb A1a1 and Hb A1a2 are adducts of sugar phosphates at the N-terminus of the beta chain. Hb A1b contains an unidentified nonphosphorylated sugar at the beta N-terminus. In addition, a significant portion of the major hemoglobin component (Hb Ao) is also glycosylated by a glucose ketoamine linkage at other sites on the molecule, including the N-terminus of the alpha chain and the epsilon-amino group of several lysine residues on both the alpha and the beta chains. The results indicate that the interaction of glucose and hemoglobin is rather nonspecific and suggests that other proteins are modified in a similar fashion.
人溶血产物中含量最丰富的次要血红蛋白成分是Hb A1c，它通过酮胺键将葡萄糖结合到β链的N端。Hb A1c在红细胞120天的寿命期间缓慢且持续形成。它可以通过将纯化的血红蛋白与14C -葡萄糖一起孵育在体外合成。其他次要成分，Hb A1a1和Hb A1a2是β链N端的糖磷酸加合物。Hb A1b在β N端含有一种未鉴定的非磷酸化糖。此外，主要血红蛋白成分（Hb Ao）的很大一部分也通过分子上其他位点的葡萄糖酮胺键进行糖基化，包括α链的N端以及α链和β链上几个赖氨酸残基的ε -氨基。结果表明葡萄糖与血红蛋白的相互作用相当非特异性，并表明其他蛋白质也以类似方式被修饰。
