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Journal of Experimental Biology, Vol 201, Issue 19 2685-2690, Copyright © 1998 by Company of Biologists

JOURNAL ARTICLES

Interaction between haemoglobin and synthetic peptides of the N-terminal cytoplasmic fragment of trout band 3 (AE1) protein

FB Jensen, MH Jakobsen and RE Weber
Institute of Biology, Odense University, DK-5230 Odense M, Denmark. fbj@biology.ou.dk

Two acidic peptides corresponding to the first 10 and 20 amino acid residues of the N-terminal, cytoplasmic fragment of rainbow trout band 3 (AE1) protein were synthesised in order to study their interaction with trout and human haemoglobin (Hb). The peptides did not influence the oxygen affinity of the main anodic trout Hb component (Hb IV) when tested at surplus peptide concentration ([peptide]/[Hb4]=16), at high and low ionic strength and at pH values ranging from 6.5 to 7.6. With human Hb, however, the 20-mer peptide markedly decreased the oxygen affinity and increased the Bohr effect. These data suggest that the trout band 3 peptide binds preferentially to the deoxy (T) conformation of human Hb, probably at the organic phosphate binding site in the central cavity between the beta-chains, which is known to be the binding site for the acidic N terminus of human band 3. In trout Hb IV, the presence of negatively charged Asp at position NA2 of the beta-chains (in contrast to positive or neutral residues in mammalian Hb) may weaken any interaction with the highly negatively charged peptides.
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