Proc Natl Acad Sci U S A
August 1991
The complete amino acid sequence of a 55-kDa erythrocyte membrane protein was deduced from cDNA clones isolated from a human reticulocyte library. This protein, p55, is copurified during the isolation of dematin, an actin-bundling protein of the erythrocyte membrane cytoskeleton. Fractions enriched in p55 also contain protein kinase activity that completely abolishes the actin-bundling property of purified dematin in vitro.
View Article and Find Full Text PDFTwo recently published reports have described findings which will have a profound impact on the understanding of molecular mechanisms of human resistance to malaria infection. In Melanesian ovalocytosis, a genetic polymorphism found in Papua New Guinea and parts of South East Asia, the red cells are highly resistant to invasion by various species of malaria parasite. The molecular nature of the defect in ovalocytic erythrocytes was not known.
View Article and Find Full Text PDFThe expression of avian erythrocyte dematin (protein 4.9) was studied in short-term tissue culture and in vivo in chickens. Our results show that erythrocyte dematin consists of five immunoreactive variants of 44, 47, 49, 50, and 52 kDa which are differentially synthesized and accumulated during avian embryonic development.
View Article and Find Full Text PDFWe used chicken alpha spectrin as a ligand probe to isolate Drosophila beta spectrin cDNA sequences from a lambda gt11 expression library. Analysis of 800 residues of deduced amino acid sequence at the amino-terminal end revealed a strikingly conserved domain of integral of 230 residues that shows a high degree of sequence similarity to the amino-terminal domains of alpha actinin and dystrophin. This conserved domain constitutes a new diagnostic criterion for spectrin-related proteins and allows the known properties of one of these proteins to predict functional properties of the others.
View Article and Find Full Text PDFA partially purified preparation of human erythrocyte protein 4.9, consisting of 48-, 52-, and 55-kilodalton polypeptides, is capable of bundling rabbit muscle actin in vitro (Siegel, D. L.
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