Spontaneous thioester bond formation in alpha 2-macroglobulin, C3 and C4.
FEBS Lett
; 308(3): 280-2, 1992 Aug 24.
Article
en En
| MEDLINE
| ID: mdl-1380468
ABSTRACT
Purified alpha 2-macroglobulin and complement proteins C3 and C4 were treated with ammonia to break their intramolecular thioester bonds and reform the original free cysteinyl and glutamyl side chains. When this reaction was performed at low temperature a conformational intermediate was trapped which lacked a thioester, but which could refold to the native structure and spontaneously reform the thioester and full biological function. The findings suggest that these proteins may undergo spontaneous post-translational self-modification forming the thioesters without involvement of enzymes or high energy metabolites such as ATP.
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Banco de datos:
MEDLINE
Asunto principal:
Alfa-Macroglobulinas
/
Complemento C3
/
Complemento C4
Límite:
Humans
Idioma:
En
Año:
1992
Tipo del documento:
Article