The incorporation of 32P into spectrin aggregates following incubation of erythrocytes in 32P-labelled inorganic phosphate |
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Authors: | J.C. Dunbar G.B. Ralston |
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Affiliation: | Department of Biochemistry, University of Sydney, Sydney, N.S.W. 2006 Australia |
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Abstract: | 32P was incorporated into spectrin by incubation of fresh erythrocytes with 32Pi and glucose. The dimer and tetramer aggregates revealed only covalently-bound incorporation of phosphorus, while a higher aggregate of spectrin revealed both covalent and non-covalent incorporation. The specific activity of the covalently-bound phosphorus in all oligomers was identical, suggesting that the state of association is independent of phosphorylation. The non-covalent incorporation was shown to be due to the association of ATP with this higher aggregate. The nucleotide appears not to be bound directly to spectrin but rather to component 5 (erythrocyte actin) which is also found to be associated with this highly aggregated spectrin structure. |
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