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L Morle, M Garbarz, N Alloisio, R Girot, I Chaveroche, P Boivin and J Delaunay
In a previous report (Blood 60:265, 1982), we described a family with an
abnormal RBC membrane protein doublet, which we considered a shortened
protein 4.1 on the basis of biochemical and genetic data. Using an anti-4.1
monoclonal antibody, we confirm here that the shortened protein derives
from protein 4.1. One of the members of the family contemporaneously
displayed the 4.1 (-) trait, eg, the heterozygous state of this variety of
hereditary elliptocytosis that lacks protein 4.1. The 4.1a/4.1b ratio was
low whenever the 4.1 trait was present, regardless of the type of protein
4.1 involved. The RBCs of the compound heterozygote, containing only the
shortened species of protein 4.1, made it possible to analyze without
interference the contact between shortened protein 4.1 and
sialoglycoprotein beta, or glycoconnectin. Shortened protein 4.1 did not
alter the amount of glycoconnectin in the ghosts nor did it change its
extractability into the Triton shells. Limited proteolysis of shortened
polypeptides 4.1a and 4.1b showed that they are sequence related. It is
conflicting that the persons carrying the shortened protein 4.1 are devoid
of specific clinical and morphological abnormalities, apart from those
pertaining to the 4.1- trait, when the latter is present.
This article has been cited by other articles:
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| Copyright © 1985 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
