Comparison of intrinsic stabilities of free and bound enzymes by graphical removal of diffusional effects.
Biochim Biophys Acta
; 485(1): 29-36, 1977 Nov 23.
Article
em En
| MEDLINE
| ID: mdl-911865
ABSTRACT
The enhanced stability usually exhibited by enzymes after immobilization may be attributed either to a stabilization effect of the solid matrix on the bound enzyme molecule or to the influences of diffusional limitations on the observed activity. To allow the comparison of the intrinsic statilities of free and bound enzymes a simple graphical procedure for the removal of external diffusional effects of stability curves is described. It is based on the determination of substrate concentration differences between the enzyme micro- and macroenvironment. Application of the method to aspartate aminotransferase bound to collagen membranes indicates that diffusional limitations for oxaloacetate are partly responsible for the observed stability enhancement. Comparison of the graphically obtained intrinsic profile with the stability curve of the soluble enzyme further demonstrate that the binding itself greatly increases the stability of aspartate aminotransferase.
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Base de dados:
MEDLINE
Assunto principal:
Aspartato Aminotransferases
/
Enzimas Imobilizadas
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1977
Tipo de documento:
Article