Enoki Y, Ohga Y, Sakata S, Kohzuki H, Shimizu S
Hemoglobin. 1986;10(6):607-21. doi: 10.3109/03630268609036565.
Structural and functional studies of minor glycosylated hemoglobins in non-human mammals have been very few. Therefore, we attempted further characterization of a canine glycosylated hemoglobin (tentatively designated as Hb Can AIc) which had been isolated by Bio-Rex 70 chromatography (Enoki, Y. et al. (1982) Hemoglobin 6, 143-151). After isolation of the constituent subunits by hybridization-mercuration technique, we found by peptide mapping that the structural modification was confined in amino-termini of the beta subunits in which glycosyl ketoamine linkage was also shown to be localized by thiobarbituric acid reaction. Compared with the major hemoglobin (Hb Can A0), Hb Can AIc was characterized by such functional properties as a slightly lower oxygen affinity and a markedly reduced response to the allosteric effects of carbon dioxide and organic phosphates. The anion and H+ Bohr effects were not different from those in Hb Can A0. All these facts support that this hemoglobin is a canine counterpart of Hb AIc.
对非人类哺乳动物中次要糖化血红蛋白的结构和功能研究非常少。因此，我们尝试进一步鉴定一种通过Bio-Rex 70色谱法分离得到的犬糖化血红蛋白（暂定为Hb Can AIc）（榎木，Y.等人（1982年）《血红蛋白》6，143 - 151）。通过杂交 - 汞化技术分离出组成亚基后，我们通过肽图谱分析发现结构修饰局限于β亚基的氨基末端，硫代巴比妥酸反应也表明糖基酮胺键定位于此。与主要血红蛋白（Hb Can A0）相比，Hb Can AIc具有如下功能特性：氧亲和力略低，对二氧化碳和有机磷酸盐变构效应的反应明显降低。阴离子和H + 玻尔效应与Hb Can A0中的无异。所有这些事实都支持这种血红蛋白是Hb AIc的犬类对应物。
