Separation of the M and N blood-group antigens of the human erythrocyte

G.M.W. Cook, E.H. Eylar
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引用次数: 86

Abstract

Treatment of washed human erythrocytes with the proteolytic enzyme pronase rapidly releases bound sialic acid from the membrane. The amount of bound sialic acid liberated is equal to the amount of free sialic acid which is released from this cell by neuraminidase (EC 3.2.1.18).

The bound sialic acid, liberated by pronase, was shown to be present in glycopeptides possessing M and N blood-group activity towards rabbit and human antisera. Using an MN active glycopeptide fraction, purified on Sephadex G-25, it has been possible by using DEAE-Sephadex to separate for the first time the M antigen from the N antigen. These glycopeptides which were obtained in a high degree of purity were shown to possess different carbohydrate compositions.

人红细胞M、N血型抗原的分离
用蛋白水解酶pronase处理洗过的人红细胞,可迅速从细胞膜释放结合的唾液酸。释放的结合唾液酸的量等于神经氨酸酶从细胞释放的游离唾液酸的量(EC 3.2.1.18)。结合的唾液酸被pronase释放,被证明存在于对兔和人抗血清具有M和N血型活性的糖肽中。使用Sephadex G-25纯化的MN活性糖肽片段,DEAE-Sephadex首次可以从N抗原中分离出M抗原。这些高纯度的糖肽被证明具有不同的碳水化合物组成。
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