Protection of a restriction enzyme from heat inactivation by [alpha]-crystallin.
Mol Vis
; 4: 29, 1998 Dec 15.
Article
em En
| MEDLINE
| ID: mdl-9873067
ABSTRACT
PURPOSE:
To determine whether the chaperone activity of human alpha-crystallin can protect a restriction enzyme from heat inactivation.METHODS:
The restriction enzyme Nde I was heated in the presence or absence of purified bovine alpha-crystallin. Following heat treatment, the enzymatic activity of the heat treated samples was assayed by cleavage of plasmid DNA. The extent of digestion was monitored by agarose gel electrophoresis and visualization of DNA fragments by ethidium bromide staining.RESULTS:
Heating of Nde I in the absence of alpha-crystallin resulted in inactivation. However, Nde I heated in the presence of alpha-crystallin remained active. Furthermore, an increased amount of alpha-crystallin provided a longer period of thermal protection.CONCLUSIONS:
The chaperone activity and thermo-protective effect of alpha-crystallin extend to protection of enzymatic activity, not merely the protection from thermally induced aggregation/denaturation. In addition, inclusion of alpha-crystallin during some enzymatic reactions may be beneficial.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Desoxirribonucleases de Sítio Específico do Tipo II
/
Chaperonas Moleculares
/
Cristalinas
Limite:
Animals
Idioma:
En
Revista:
Mol Vis
Assunto da revista:
BIOLOGIA MOLECULAR
/
OFTALMOLOGIA
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
Estados Unidos