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Spectrin current understanding of its physical biochemical and functional properties

, : Spectrin current understanding of its physical biochemical and functional properties. Life Sciences 19(1): 1-18

Spectrin consists of a complex of 2 peptides (bands 1 and 2) which have MW of about 240,000 and 220,000 daltons (.+-. 10% or more). Aggregation states of dimer, tetramer and high polymer appear to be favored. Each of the 2 bands contains multiple isoelectric, antigenic and N-terminal components; it is not known if this phenomenon is due to natural multiplicity, to proteolysis, or to the presence of non-SDS[sodium dodecyl sulfate]-dissociable subunits. Compared to myosin, the spectrin dimer is probably somewhat less .alpha.-helical and somewhat more globular. Spectrin has a weak ATPase activity which shows distinguishable Mg-ATPase and Ca-ATPase components, and band 2 of spectrin is phosphorylated by ATP-.gamma.-32P under physiologic conditions. Spectrin is present in vivo as a complex with erythrocytic actin, and after isolation will form complexes with muscle actin. The nature of these complexes is still uncertain. Spectrin interacts both with lipid bilayers (devoid of intrinsic proteins) and with the intrinsic proteins of the erythrocyte and binds Ca and ATP under appropriate conditions. These properties make it likely that spectrin controls the membrane deformability of erythrocyte (via unknown regulatory mechanisms) and is an essential component of the erythrocyte membrane in terms of its stability as an extended, flat and elastic surface. There is fragmentary evidence suggesting spectrin-like proteins exist in membranes from other cell types and possibly in cytoplasm.

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Accession: 006459997

PMID: 133279

DOI: 10.1016/0024-3205(76)90368-4

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