Substitution of alanine543 with a threonine residue at the carboxy terminal end of the beta-chain is associated with thermolabile hexosaminidase B in a Jewish family of Oriental ancestry.
Biochem Mol Med
; 56(1): 31-6, 1995 Oct.
Article
en En
| MEDLINE
| ID: mdl-8593535
ABSTRACT
Thermolabile forms of the lysosomal enzyme beta-hexosaminidase B (Hex B), likely to result from different genetic defects, have been described. Ten individuals in five generations of a family of Oriental Jewish ancestry were identified biochemically as carriers of a thermolabile Hex B form. The beta-chain thermolability was found to be associated with the presence of a G --> A transition at nucleotide 1627 of the HEX B gene causing the substitution of Ala543 with a threonine. Oriental Jew whose Hex B was heat labile. Since thermolabile Hex B has been shown to occur more frequently among Jews of Oriental origin, the Ala543 --> Thr mutation may be the common mutation associated with beta-chain thermolability in this ethnic group.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Treonina
/
Beta-N-Acetilhexosaminidasas
/
Judíos
/
Alanina
Tipo de estudio:
Risk_factors_studies
Límite:
Female
/
Humans
/
Male
País/Región como asunto:
Asia
Idioma:
En
Revista:
Biochem Mol Med
Asunto de la revista:
BIOQUIMICA
Año:
1995
Tipo del documento:
Article
País de afiliación:
Estados Unidos