Red cell membrane protein anomalies in XXXX (HEMP AS).

@entity154 @entity417 @entity10644 @entity535 @entity1735 @entity4843 @entity214
In all of six cases of @entity417 ( @entity4843 ), gel electrophoresis in the presence of @entity214 revealed abnormally rapid migration of the preponderant integral membrane protein, band 3. After proteolysis of intact cells, the remaining part of the band 3, comprising the intramembrane segment and the cytoplasmic domain, migrated electrophoretically as a single band, identical in mobility to that from normal cells treated in the same manner. The @entity154 thus resides in the extracellular domain of the protein, which is the glycosylated part of the chain. Peptide digests of the band 3 showed no evidence of a missing protein segment in the abnormal cells and the @entity535 composition of the peptides derived from proteolysis of the extracellular protein of intact cells was also normal. We infer that the @entity154 is one of glycosylation. The major glycoproteins, detected by @entity1735 -specific (PAS) stain appear normal in SDS gels. However, when the more sensitive procedure of reacting after electrophoresis with radioiodinated lentil lectin is employed, some additional minor protein components are revealed. In particular one species of apparent subunit molecular weight about 150 000 appeared in all cases of @entity4843 examined and in no normals. This component is not accessible to proteolysis by chymotrypsin or @entity10644 protease, and may be associated with the inner membrane patches, characteristic of the @entity4843 . Overall cell shape and microviscosity of the membrane bilayer, as measured by fluorescence polarization of a lipid-soluble fluorophore, were substantially normal in @entity4843 cells.
