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Spectrin bands 1 and 2 are antigenically distinct and are not composed of subunits


, : Spectrin bands 1 and 2 are antigenically distinct and are not composed of subunits. Archives of Biochemistry and Biophysics 186(1): 1-8

Human erythrocyte membranes and freshly isolated spectrin were separated into their constituent peptides by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The peptides were electrophoresed from slices of such gels into agarose gels containing anti-spectrin antibodies and Triton X-100. In fresh preparations, precipitin arcs were observed only against peptides migrating as bands 1 and 2. Bands 1 and 2 did not cross-react. There were 2 major arcs from band 1 and 1 principal arc from band 2, plus minor splitting of these arcs. None of the band 1 arcs fused with band 2 arcs. In fresh erythrocyte ghosts, only bands 1 and 2 reacted with anti-spectrin; bands 2.1, 3 and 5, in particular, showed no precipitin arcs. In aged ghosts, arcs appeared in the band 3 region; in aged isolated spectrin, arcs appeared in the band 2.1 region; and in trypsin-degraded spectrin, reactive species occurred in all MW classes. Spectrin has no subunits smaller than 220,000 MW. Bands 1 and 2 are immunochemically distinct.

Accession: 006459994

PMID: 75713

DOI: 10.1016/0003-9861(78)90456-3

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Related references

Kirkpatrick, F.H.; Rose, D.J.; L.C.lle, P., 1978: Spectrin band 1 and 2 are antigenically distinct and are not composed of subunits. Archives of Biochemistry and Biophysics 186(1): 1-8

Davis, J.; Bennett, V., 1983: Brain spectrin. Isolation of subunits and formation of hybrids with erythrocyte spectrin subunits. Brain spectrin tetramer was purified from pig brain membranes in milligram quantities. The tetramer had subunits of Mr = 265,000 (alpha) and Mr = 260,000 (beta), Rs = 21.4 nM, S20,w = 11 S, V = 0.725 ml/g, frictional ratio of 2.9, and calculated m...

Clark, M.B.; Goodman, S.R., 1993: Neuronal compartmentalization demonstrates distinct alpha subunits of brain spectrin isoforms. Molecular Biology of the Cell 4(SUPPL ): 172A

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Woods C.M.; Lazarides E., 1985: Degradation of unassembled alpha spectrin and beta spectrin by distinct intracellular pathways regulation of spectrin topogenesis by beta spectrin degradation. Analysis of the turnover of unassembled proteins during the assembly of the erythroid membrane skeleton has revealed that .alpha.- and .beta.-spectrin 2 structurally related, high MW proteins, are degraded in a selective manner by 2 distinct intra...

Tyler, J.M.; Hargreaves, W.R.; Branton, D., 1979: Purification of two spectrin-binding proteins: biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1. Two peripheral proteins of the human erythrocyte membrane that are capable of forming a stable complex with spectrin have been purified. The proteins, band 2.1 (Mr 210,000) and band 4.1 (Mr 82,000), are water soluble and exist as monomers in solut...

Tyler, J.M.; Hargreaves, W.R.; Branton, D., 1979: Purification of 2 spectrin binding proteins biochemical and electron microscopic evidence for site specific reassociation between spectrin and bands 2.1 and 4.1. Two peripheral proteins of the human erythrocyte membrane that are capable of forming a stable complex with spectrin were purified. The proteins, band 2.1 (MW 210,000) and band 4.1 (MW 82,000), are water soluble and exist as monomers in solution....

Riederer, B.M.; Zagon, I.S.; Goodman, S.R., 1986: Brain spectrin(240/235) and brain spectrin(240/235E): two distinct spectrin subtypes with different locations within mammalian neural cells. Adult mouse brain contains at least two distinct spectrin subtypes, both consisting of 240-kD and 235-kD subunits. Brain spectrin(240/235) is found in neuronal axons, but not dendrites, when immunohistochemistry is performed with antibody raised a...

Anderson, J.M., 1979: Structural studies on human spectrin. Comparison of subunits and fragmentation of native spectrin. Native spectrin has trypsin-susceptible sites spaced at a constant molecular weight interval. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of spectrin treated with trypsin at low salt concentrations shows a ladder of fragments spaced...

Kasturi, K.; Fleming, J.; Harrison, P., 1983: A monoclonal antibody against erythrocyte spectrin reacts with both a- and b-subunits and detects spectrin-like molecules in non-erythroid cells. Experimental Cell Research 144: 1-7