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Weak n activity of en(a−) human erythrocyte membranes
Author(s) -
Shinozuka Tatsuo,
Miyata Yoshihisa,
Ohyama Kunio,
Takei Setsuko,
Yamakawa Toshio,
Kurihara Katsuyoshi,
Yanagida Junichi
Publication year - 1993
Publication title -
american journal of hematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.456
H-Index - 105
eISSN - 1096-8652
pISSN - 0361-8609
DOI - 10.1002/ajh.2830440313
Subject(s) - membrane , chemistry , medicine , biochemistry
Abstract The propositus's erythrocytes with phenotype En(a−), which was found for the first time in a Japanese family, reacted more weakly with anti‐N serum than the ordinary phenotype N erythrocytes. The En(a−) erythrocytes lack the major membrane sialoglycoprotein (glycophorin A) as demonstrated by Bio‐Gel 1.5m gel filtration from active sialoglycoproteins, which were isolated from En(a−) erythrocyte membranes by the method of lithium diiodosalicylate (LIS)‐phenol extraction. It is suggested from observation via enzymelinked immunosorbent assay (ELISA) that N activity is derived from the glycophorin B molecule on En(a−) erythrocyte membranes. © 1993 Wiley‐Liss, Inc.