Differentiation of the contribution of the two subunits of lutropin to its in vivo activity.
Biochim Biophys Acta
; 533(1): 257-62, 1978 Mar 28.
Article
en En
| MEDLINE
| ID: mdl-565219
ABSTRACT
Porcine and ovine lutropins were acetimidated at amino groups to various degrees and the effects of the modification on the induction of ovarian ornithine decarboxylase activity were examined. A drastic (84%) loss of biological activity was observed upon modification of two amino groups in porcine lutropin. The results with ovine lutropin derivatives were quite similar. Circular dichroism measurements showed no conformational changes and dissociation into subunits was not observed in the derivatives. Accordingly, the loss of biological activity was not a by-product of conformational changes. It was concluded that lutropin carries a single binding site which is constructed by surface residues or regions located on both the alpha- and beta-subunits of the hormone.
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Banco de datos:
MEDLINE
Asunto principal:
Hormona Luteinizante
Límite:
Animals
Idioma:
En
Año:
1978
Tipo del documento:
Article