Tondo C V
Hemoglobin. 1976;1(2):195-210. doi: 10.3109/03630267608991680.
Hemoglobin Porto Alegre is an abnormal human hemoglobin which polymerizes by formation of intermolecular disulfide bonds between the mutant cysteinyl residues at the beta9 position. Biochemical studies of this abnormal hemoglobin from a heterozygous carrier of a second family of carriers indicates that an asymmetric tetramer alphaA2betaAbeta9 Ser replaces Cys is formed after polymerization. Functional studies of the polymer indicate that its oxygen binding properties are unaffected by the polymerization and that its oxygen affinity is somewhat higher than that of normal hemoglobin; it has a slightly reduced heme-heme interaction and a normal Bohr effect.
阿雷格里港血红蛋白是一种异常的人类血红蛋白，它通过在β9位置的突变半胱氨酸残基之间形成分子间二硫键而发生聚合。对来自第二个携带者家族的杂合子携带者的这种异常血红蛋白的生化研究表明，聚合后形成了一种不对称四聚体αA2βAβ9丝氨酸取代半胱氨酸。对该聚合物的功能研究表明，其氧结合特性不受聚合影响，且其氧亲和力略高于正常血红蛋白；其血红素-血红素相互作用略有降低，具有正常的玻尔效应。
