Zak S J, Geller G R, Krivit W, Tukey D, Brimhall B, Jones R T, Bunn H F, McCormack M
Br J Haematol. 1976 May;33(1):101-4. doi: 10.1111/j.1365-2141.1976.tb00975.x.
Haemoglobin Malmöbeta97His leads to Gln, a high oxygen affinity haemoglobin which causes secondary erythrocytosis, is transmitted in an autosomal dominant manner. A hypothesis accounting for the high oxygen affinity, hyperbolic oxyhaemoglobin dissociation curve, and the relatively normal Bohr effect is presented. The purified abnormal haemoglobin from the present family provided biochemical and functional data for this hypothesis based on the allosteric model proposed by Perutz. Experimental results support the formation of a chemical bond between the -SH proton of the beta93 cysteine and the amide of oxygen of the substituted beta97 glutamine as an explanation for the high oxygen affinity of haemoglobin Malmö.
血红蛋白马尔默β97His突变为谷氨酰胺，形成一种高氧亲和力血红蛋白，可导致继发性红细胞增多症，呈常染色体显性遗传。本文提出了一个假说来解释其高氧亲和力、双曲线型氧合血红蛋白解离曲线以及相对正常的波尔效应。从该家族中纯化得到的异常血红蛋白，基于佩鲁茨提出的别构模型，为这一假说提供了生化和功能数据。实验结果支持β93半胱氨酸的-SH质子与取代的β97谷氨酰胺的氧酰胺之间形成化学键，以此解释血红蛋白马尔默的高氧亲和力。
