一篇关于一个家族病史中罕见的红细胞增多症的研究，通过创新的电泳和色谱技术，识别出名为Hb Malm的异常血红蛋白。研究显示其独特的生理特性，包括正常Bohr效应和低温下较低的氧亲和力。关键发现聚焦于FG-4位点的氨基酸替换，区别于Chesapeake血红蛋白，但影响β链而非α链。携带者表现出显著的血液异常。
摘要：
A striking history of familial polycythemia led to a search for an abnormal hemoglobin. None could be demonstrated by routine electrophoretic methods, but the propositus' hemolysate had increased oxygen affinity. Manipulation of the conditions of electrophoresis, and chromatographic methods, permitted identification of hemoglobin Malm. Studies of hemolysates demonstrated a normal Bohr effect, decreased heme-heme interaction (n=1.58), and a p50 of 1.3 mm Hg at 10 degrees C and pH 7.2. The amino acid substitution occurs in the same position (FG-4) as that of hemoglobin Chesapeake, but in the beta-chain rather than the alpha-chain. The two types of hemolysate have different pathophysiologic properties, and carriers of hemoglobin Malm exhibit more striking hematologic abnormalities.
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