Structural analysis, fatty acid and thyroxine binding properties of Vancouver and Naskapi variants of human serum albumin.
Clin Biochem
; 36(8): 597-605, 2003 Nov.
Article
en En
| MEDLINE
| ID: mdl-14636873
ABSTRACT
OBJECTIVES:
To purify and structurally identify two albumin variants found in the Canadian population of native Amerindian origin. To assess the ability of variant albumins to bind lauric acid and L-thyroxine.METHODS:
The structural characterization of the alloalbumins was performed by conventional protein chemistry methods and by mass spectrometric analysis. Lauric acid and L-thyroxine affinities to variant albumins were assessed by kinetic dialysis and equilibrium dialysis techniques, respectively.RESULTS:
The sequence investigations proved the two variants to be albumin Naskapi [372Lys --> Glu] and albumin Vancouver [501Glu --> Lys], respectively. Among the carriers of albumin Naskapi, we found a rare case of homozygosity. Furthermore, this is the first reported case of the 501Glu-->Lys mutation in the native North American population. Scatchard plot analysis revealed that the association constants for lauric acid and L-thyroxine to the two variants were indistinguishable from the endogenous form of albumin.CONCLUSION:
We show that albumin variants Vancouver and Naskapi have normal fatty acid and L-thyroxine binding capabilities. These findings support the assumption that bisalbuminemias associated with these albumin variants are benign conditions.
Buscar en Google
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Tiroxina
/
Variación Genética
/
Albúmina Sérica
/
Ácidos Grasos
Tipo de estudio:
Prognostic_studies
Límite:
Humans
País/Región como asunto:
America do norte
Idioma:
En
Revista:
Clin Biochem
Año:
2003
Tipo del documento:
Article
País de afiliación:
Italia