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• W1968941618 abstract "We have identified a rabbit autoantibody that strongly reacts with the core membrane skeleton of control red blood cells, and does not react with low- or high-density sickle cell core skeletons upon indirect immunofluorescence. Western blot analysis of red blood cell membrane proteins, utilizing this autoantibody, indicated no reactivity to any protein when SDS-PAGE was conducted in the presence of the reducing agent, dithiothreitol. However when SDS-PAGE was performed on control red blood cell membrane proteins separated in the absence of dithiothreitol, the autoantibody specifically reacted with a high molecular weight polypeptide (apparent Mr ≊ 310 kD) representing a DTT sensitive form of control α spectrin, which we refer to as α/ spectrin. There was no staining of high density or low density sickle cell α or α/ spectrin. This autoantibody should be an excellent tool for the fine mapping of structural change(s) in control vs. sickle cell α spectrin, and determination of whether the structural alteration effects spectrin dimer-tetramer interconversion and/or the spectrin-actin interaction. The modification in α spectrin, detected by this antibody, is very specific for homozygous SS α spectrin because sickle cell β+ thalassemic α spectrin and sickle cell trait α spectrin react intensely with the autoantibody. Am. J. Hematol. 58:200–205, 1998. © 1998 Wiley-Liss, Inc." @default.
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• W1968941618 date "1998-07-01" @default.
• W1968941618 modified "2023-09-23" @default.
• W1968941618 title "Preliminary characterization of a structural defect in homozygous sickled cell alpha spectrin demonstrated by a rabbit autoantibody" @default.
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• W1968941618 doi "https://doi.org/10.1002/(sici)1096-8652(199807)58:3<200::aid-ajh7>3.0.co;2-v" @default.
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