Thermodynamic characterisation of the mutated isoenzyme A of beta-N-acetylhexosaminidase in GM2-gangliosidosis B1 variant.
Clin Chim Acta
; 285(1-2): 45-51, 1999 Jul.
Article
em En
| MEDLINE
| ID: mdl-10481922
ABSTRACT
Here we report the determination of the activation energies of the plasma isoenzymes of beta-N-acetylhexosaminidase (Hex, EC 3.2.1.52), isolated by chromatography in DEAE-cellulose, using the neutral chromogenic substrate 3,3'dichlorophenylsulfonphthaleinyl-N-acetyl-beta-D-glucosaminide. The activation energy of mutated Hex A isoenzyme (Ea approximately 71.5 kJ/mol) from a patient with GM2-gangliosidosis B1 variant, homozygote for the G533-->A (Arg178His) mutation, was significantly higher than that of normal Hex A (Ea approximately 41.8 kJ/mol) and analogous to that of Hex B isoenzyme (Ea approximately 75.1 kJ/mol). The determination of this thermodynamic variable of Hex in different biological specimens could allow for a straightforward biochemical characterisation of the GM2-gangliosidosis B1 variant.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Beta-N-Acetil-Hexosaminidases
/
Gangliosidoses
/
Mutação Puntual
/
Isoenzimas
Limite:
Child
/
Female
/
Humans
Idioma:
En
Ano de publicação:
1999
Tipo de documento:
Article