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The desialization of glycoproteins increased their activity toward anti\u2010I<jats:sup>S<\/jats:sup> and anti\u2010I<jats:sup>D<\/jats:sup> sera, and did not change or decreased the activity toward anti\u2010I<jats:sup>F<\/jats:sup> sera. The most abundant fraction II (major sialoglycoprotein of erythrocyte membranes) showed no or only a very weak I activity, but I\u2010active glycopeptides were isolated from products of digestion of fraction II with trypsin. The major product of digestion, sialoglycopeptide IIT\u20102 showed I activity only after alkaline elimination of alkali\u2010labile oligosaccharide chains. The results indicate that I receptors are present in hindered form on apparently I\u2010inactive components of erythrocyte membrane.<\/jats:p>","DOI":"10.1111\/j.1423-0410.1975.tb02750.x","type":"journal-article","created":{"date-parts":[[2009,3,6]],"date-time":"2009-03-06T01:41:23Z","timestamp":1236303683000},"page":"122-132","source":"Crossref","is-referenced-by-count":15,"title":["Reactions of Erythrocyte Glycoproteins and their Degradation Products with various Anti\u2010I Sera"],"prefix":"10.1111","volume":"28","author":[{"given":"Elwira","family":"Lisowska","sequence":"first","affiliation":[]},{"given":"Wanda","family":"Dzier\u017akowa\u2010Borodej","sequence":"additional","affiliation":[]},{"given":"Halina","family":"Seyfried","sequence":"additional","affiliation":[]},{"given":"Zofia","family":"Drzeniek","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2009,3,5]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(69)90896-1"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj1380381"},{"key":"e_1_2_1_4_2","first-page":"631","article-title":"Studies on blood group antigens M and N. 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