Sickle cell hemoglobin fiber structure altered by alpha-chain mutation.
Proc Natl Acad Sci U S A
; 78(3): 1406-10, 1981 Mar.
Article
en En
| MEDLINE
| ID: mdl-6940165
Hybrid hemoglobin molecules prepared with beta chains from hemoglobin S (beta 6 Glu leads to Val) and alpha chains from hemoglobin Sealy (alpha 47 Asp leads to His) form fibers with a novel structure. In contrast to the typical fibers of hemoglobin S with an average diameter of 22 nm and a solid cross section composed of 10 outer filaments surrounding a 4-filament core, the fibers of the alpha Sealy2 beta S2 hybrid are much larger, with a mean diameter of 32 nm and a unique double-hollow arrangement of filaments. Sealy--S fibers can be described by a model in which the two pairs of filaments most readily lost from fibers of hemoglobin S are missing to form the hollow regions, with an additional sheath of filaments added to form the overall larger structure.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Hemoglobina Falciforme
/
Mutación
Límite:
Humans
Idioma:
En
Revista:
Proc Natl Acad Sci U S A
Año:
1981
Tipo del documento:
Article
Pais de publicación:
Estados Unidos