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An anti‐En a TS detected in the serum of an Mi I homozygote
Author(s) -
Spruell P.,
Moulds J.J.,
Martin M.,
Gilcher R.O.,
Howard P.B.,
Blumenfeld O.O.
Publication year - 1993
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1046/j.1537-2995.1993.331094054625.x
Subject(s) - sialoglycoprotein , microbiology and biotechnology , glycoprotein , gel electrophoresis , sialoglycoproteins , spectrin , trypsin , polyacrylamide gel electrophoresis , chemistry , red blood cell , heterozygote advantage , biology , biochemistry , gene , allele , enzyme , cell , cytoskeleton
The serum of EH reacted with all red cells (RBCs) except her own, ficin‐ or trypsin‐treated red cells, and En(a‐) red cells. This reactivity defined an anti‐En a TS specificity. The red cells of the proposita typed as M‐N+S‐S+, Vw+Mur‐Hil‐Hut‐Anek‐Lane‐, Wr(a‐b+), En a KT+. Red cells of five relatives were Vw+ and positive with her serum. Titration studies suggest that EH is genetically an Mi I homozygote and that her Vw+ relatives are Mi I heterozygotes. There is no history of consanguinity. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and immunoblotting studies have agreed with the serologic observations. A variant sialoglycoprotein of faster mobility than normal glycoprotein A, but no normal glycoprotein A, was detected on her red cells. Treatment with N‐glycanase did not alter the mobility, which indicated that there was no N‐glycosylation of residue 26. These findings are in agreement with the reported properties of the Mi.I‐specific glycoprotein A. The relatives' Vw+ red cells showed the variant sialoglycoprotein and normal glycoprotein A. EH appears to be the first reported Mi I homozygote.