Johnson C S, Schroeder W A, Shelton J B, Shelton J R
Hemoglobin. 1983;7(2):125-40. doi: 10.3109/03630268309048642.
Hemoglobin Boyle Heights (alpha 6 (A4) Asp leads to O) is the first observed variant with a deletion in the alpha chain. The variant, which was detected in a 39-year-old man of Mexican descent, constitutes 14% of the total hemoglobin and is associated with microcytosis, heat instability, and increased oxygen affinity. It migrates between Hb F and Hb S on cellulose acetate and starch gel electrophoresis and with Hb A on citrate agar gel electrophoresis. Identification was done by high performance liquid chromatographic procedures. Residue Asp alpha 6 is neither a heme nor an interchain contact, but does have intrachain contacts. Like Hb Sawara (alpha 6 Asp leads to Ala), Hb Boyle Heights has increased oxygen affinity. It is likely that the Bohr effect will be altered because the deletion in Hb Boyle Heights should alter the configuration of Val alpha 1 and influence its participation in the Bohr effect.
博伊尔高地血红蛋白（α6（A4）天冬氨酸导致O）是首个观察到的α链存在缺失的变体。该变体在一名39岁的墨西哥裔男性中被检测到，占总血红蛋白的14%，并与小红细胞症、热不稳定性和氧亲和力增加有关。在醋酸纤维素和淀粉凝胶电泳中，它在Hb F和Hb S之间迁移，在枸橼酸盐琼脂凝胶电泳中与Hb A迁移情况相同。通过高效液相色谱法进行鉴定。α6位的天冬氨酸残基既不是血红素也不是链间接触点，但确实存在链内接触。与泽原血红蛋白（α6天冬氨酸导致丙氨酸）一样，博伊尔高地血红蛋白的氧亲和力增加。由于博伊尔高地血红蛋白中的缺失应该会改变缬氨酸α1的构型并影响其参与玻尔效应，所以很可能玻尔效应会发生改变。
