Determination of L-lactate binding stoichiometry and differences in allosteric interactions of structurally distinct homohexamers from Panulirus interruptus hemocyanin.
Biochim Biophys Acta
; 916(3): 376-80, 1987 Dec 18.
Article
em En
| MEDLINE
| ID: mdl-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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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Hemocianinas
/
Lactatos
Limite:
Animals
Idioma:
En
Ano de publicação:
1987
Tipo de documento:
Article