{"title":"人红细胞M、N血型抗原的分离","authors":"G.M.W. Cook, E.H. Eylar","doi":"10.1016/0926-6534(65)90030-8","DOIUrl":null,"url":null,"abstract":"<div><p>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).</p><p>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.</p></div>","PeriodicalId":100163,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Mucoproteins and Mucopolysaccharides","volume":"101 1","pages":"Pages 57-66"},"PeriodicalIF":0.0000,"publicationDate":"1965-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6534(65)90030-8","citationCount":"86","resultStr":"{\"title\":\"Separation of the M and N blood-group antigens of the human erythrocyte\",\"authors\":\"G.M.W. Cook, E.H. Eylar\",\"doi\":\"10.1016/0926-6534(65)90030-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>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).</p><p>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.</p></div>\",\"PeriodicalId\":100163,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Mucoproteins and Mucopolysaccharides\",\"volume\":\"101 1\",\"pages\":\"Pages 57-66\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1965-03-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6534(65)90030-8\",\"citationCount\":\"86\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Mucoproteins and Mucopolysaccharides\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926653465900308\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Mucoproteins and Mucopolysaccharides","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926653465900308","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Separation of the M and N blood-group antigens of the human erythrocyte
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.
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