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Determination of L-lactate binding stoichiometry and differences in allosteric interactions of structurally distinct
B A Johnson1, J Bonaventura, C Bonaventura
1Marine Biomedical Center, Duke University Marine Laboratory, Beaufort, NC.
Biochimica Et Biophysica Acta
|December 18, 1987
Abstract:
The role of structurally distinct subunits from the hemocyanin of Panulirus interruptus was investigated by the analysis of the oxygen-binding properties of reassembled homohexamers. Homohexamers reassembled from subunits a and b exhibited cooperative oxygen binding, whereas subunit c did not. The oxygen affinity of homohexamers from subunits b and c was specifically increased by the addition of L-lactate, whereas that of subunit a was not. Both native hexamers and the homohexamers from subunit b have approximately one oxygen-linked lactate binding site per hexamer.