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  • Title: Determination of L-lactate binding stoichiometry and differences in allosteric interactions of structurally distinct homohexamers from Panulirus interruptus hemocyanin.
    Author: Johnson BA, Bonaventura J, Bonaventura C.
    Journal: Biochim Biophys Acta; 1987 Dec 18; 916(3):376-80. PubMed ID: 3689798.
    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.
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