Ovine prolactin and human growth hormone derivatives. Specific modification of their alpha-amino groups.

Caridad, J J; Nowicki, C; Santomé, J A; Wolfenstein-Todel, C

Caridad, J J; Nowicki, C; Santomé, J A; Wolfenstein-Todel, C.

Afiliação

Caridad JJ; Institute of Biochemistry and Biophysics, (UBA-CONICET), Faculty of Pharmacy and Biochemistry, Buenos Aires, Argentina.

Int J Pept Protein Res ; 31(6): 509-13, 1988 Jun.

Article em En | MEDLINE | ID: mdl-3410636

RESUMO

The alpha-amino group of ovine prolactin (oPRL) and human growth hormone (hGH) was selectively modified by transamination with glyoxylic acid. No difference was found in the binding capacity of transaminated oPRL to rat liver lactogenic receptors with respect to its control, although both samples showed a decrease in its binding capacity with reference to the native hormone. This decrease was due to conformational changes caused by the reaction conditions and not by the transamination itself, as shown by the circular dichroism spectra. Transaminated hGH retained the full binding capacity of the hormone. These results suggest that the alpha-amino group is not relevant for the binding to lactogenic liver receptors in both lactogenic hormones.

Assuntos

Hormônio do Crescimento/análogos & derivados; Hormônio do Crescimento/síntese química; Prolactina/análogos & derivados; Prolactina/síntese química; Animais; Ligação Competitiva; Dicroísmo Circular; Humanos; Cinética; Fígado/metabolismo; Prolactina/metabolismo; Conformação Proteica; Receptores da Prolactina/metabolismo; Ovinos; Relação Estrutura-Atividade

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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Prolactina / Hormônio do Crescimento Limite: Animals / Humans Idioma: En Revista: Int J Pept Protein Res Ano de publicação: 1988 Tipo de documento: Article País de afiliação: Argentina País de publicação: Dinamarca

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