Moo-Penn W F, Schneider R G, Shih T, Jones R T, Govindarajan S, Govindarajan P G, Patchen L C
Blood. 1980 Aug;56(2):246-50.
Hemoglobin Ohio [beta 142 (H20) Ala replaced by Asp] was found in three members of a white family, all of whom showed erythrocytosis. The variant hemoglobin has a high oxygen affinity, a reduced Bohr effect, and diminished cooperativity. The functional abnormalities of Hb Ohio are explained by the proximity of the substituent beta 142 residue, both to beta 143 His, which is involved in the DPG binding site of hemoglobin, and to the critical C terminal region of the beta chain, which participates in the stabilization of the deoxy (T) conformation.
在一个白人家庭的三名成员中发现了俄亥俄血红蛋白[β142（H20）位的丙氨酸被天冬氨酸取代]，他们均表现为红细胞增多症。这种变异血红蛋白具有高氧亲和力、降低的玻尔效应和减弱的协同性。俄亥俄血红蛋白的功能异常可通过取代的β142残基与参与血红蛋白二磷酸甘油酸（DPG）结合位点的β143组氨酸以及参与脱氧（T）构象稳定的β链关键C末端区域距离较近来解释。
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