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Decreased glycosylation of band 3 and band 4‐5 glycoproteins of erythrocyte membrane in congenital dyserythropoietic anaemia type II
Author(s) -
Scartezzini P.,
Forni G. L.,
Baldi M.,
Izzo C.,
Sansone G.
Publication year - 1982
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1982.tb02820.x
Subject(s) - glycoprotein , band 3 , galactose oxidase , membrane glycoproteins , glycosylation , biochemistry , membrane protein , galactose , chemistry , biology , membrane
S ummary . We report a study of HEMPAS erythrocyte membrane glycoproteins in relation to proteolytic digestion and surface labelling with galactose‐oxidase/NaB[ 3 H] 4 . The proteolytic digestion of band 3, the major intrinsic glycoprotein of the human erythrocyte membrane, reveals an abnormality in the outer glycosylated segment of this protein. 3 H incorporation in band 3 and band 4‐5 glycoproteins after treatment with galactose‐oxidase/NaB[ 3 H] 4 is reduced in HEMPAS red cells suggesting a defective glycosylation of these proteins. These findings together with the persistence of i antigen and the normal presence of I antigen lead us to conclude that erythroblastic membrane features may persist in HEMPAS erythrocytes.