Enzymological studies of melanotropins.
Comp Biochem Physiol B
; 78(3): 519-24, 1984.
Article
en En
| MEDLINE
| ID: mdl-6332706
ABSTRACT
The relative stability of natural melanotropins and related synthetic analogues to serum and purified proteolytic enzymes was studied. Both alpha- and beta-MSH were rapidly inactivated by frog serum, but much more slowly by rat serum. beta-MSH was more stable than alpha-MSH to serum inactivation. Both alpha- and beta-MSH were rapidly inactivated by alpha-chymotrypsin and trypsin. The synthetic analogues, [Nle4, D-Phe7]-alpha-MSH and [Cys4, Cys10]-alpha-MSH, were totally resistant to inactivation by frog and rat serum enzymes. [Nle4, D-Phe7]-alpha-MSH was resistant to inactivation by alpha-chymotrypsin and trypsin, whereas [Cys4, Cys10]-alpha-MSH was partially resistant to these enzymes under similar conditions. Melanotropin analogues resistant to inactivation by serum enzymes may prove useful in a variety of physiological studies wherein natural melanotropins would be rapidly inactivated.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Alfa-MSH
/
Hormonas Estimuladoras de los Melanocitos
/
Enzimas
Límite:
Animals
Idioma:
En
Revista:
Comp Biochem Physiol B
Año:
1984
Tipo del documento:
Article