Abnormal human hemoglobins IX. Chemistry of hemoglobin JBaltimore

Corrado Baglioni , David J. Weatherall
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引用次数: 55

Abstract

A human abnormal hemoglobin with the electrophoretic mobility of hemoglobin J has been isolated and studied. The amino acid substitution in this abnormal hemoglobin has been investigated. It has been found that an aspartic acid residue substitutes in this hemoglobin J the glycine residue present in position 16 of the β peptide chain. There are reasons to believe that the hemoglobin J studied is different from other hemoglobin J's. Accordingly, the hemoglobin studied has been specifically designated hemoglobin JBaltimore.

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人血红蛋白异常。血红蛋白的化学
分离并研究了一种具有血红蛋白J的电泳迁移率的人异常血红蛋白。对这种异常血红蛋白中的氨基酸取代进行了研究。在这个血红蛋白中发现一个天冬氨酸残基取代了β肽链第16位的甘氨酸残基。有理由相信所研究的血红蛋白J不同于其他血红蛋白J。因此,所研究的血红蛋白被专门命名为血红蛋白JBaltimore。
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