Correlation between unfolded states of apocytochrome c and its ability to pass lipid bilayer.
Sci China B
; 37(11): 1341-9, 1994 Nov.
Article
en En
| MEDLINE
| ID: mdl-7865125
ABSTRACT
In contrast to the horse heart apocytochrome c, the chicken heart apocytochrome c underwent a conformational change from random coil to partial folding during a renaturation process. When the apocytochrome horse heart and that of chicken heart c were subjected to a translocation assay in vitro using large trypsin-enclosed unilamellar vesicles from soybean phospholipids, the ability of the chicken heart apocytochrome c to penetrate into the liposomes was found to decrease markedly with the renaturation procedure, while that of horse heart apocytochrome c remained relatively constant. Observations from circular dichroism measurement on the induction of secondary folding of these two species of apocytochrome c upon interaction with soybean phospholipid vesicles suggested that a more flexible structure of apocytochrome c embedded in the lipid matrix be required for its efficient translocation across the bilayer.
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Banco de datos:
MEDLINE
Asunto principal:
Apoproteínas
/
Pliegue de Proteína
/
Grupo Citocromo c
Límite:
Animals
Idioma:
En
Año:
1994
Tipo del documento:
Article