Time-resolved fluorescence studies on site-directed mutants of human serum albumin.
FEBS Lett
; 408(1): 67-70, 1997 May 12.
Article
en En
| MEDLINE
| ID: mdl-9180270
Human serum albumin (HSA) contains a single tryptophan residue at position 214. The emission properties of tryptophan 214 from recombinant albumins, namely, normal HSA, FDH-HSA and a methionine 218 HSA were examined. In all cases, the excited state lifetimes were best described by a two component model consisting mainly of a Lorentzian distribution. The centers of these distributions were 5.60 ns for HSA, 4.23 ns for FDH-HSA, and 6.08 ns for Met-218 HSA. The global rotational correlation times of the three HSAs were near 41 ns while the amplitude and rate of the local motion varied. These changes in the lifetimes and mobilities suggest perturbation in the local protein environment near tryptophan 214 as a consequence of the amino acid substitutions.
Buscar en Google
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Espectrometría de Fluorescencia
/
Albúmina Sérica
/
Mutagénesis Sitio-Dirigida
Límite:
Humans
Idioma:
En
Revista:
FEBS Lett
Año:
1997
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Reino Unido