[Interaction of alpha-chymotrypsin with dimethylsulfoxide: a change of substrate could change the mechanism of interaction]. / Vzaimodeistvie alpha-khimotripsina s dimetilsul'foksidom: smeni substrat--"izmenish'" mekhanizm vzaimodeistvii.
Bioorg Khim
; 29(5): 479-85, 2003.
Article
em Ru
| MEDLINE
| ID: mdl-14601402
ABSTRACT
The kinetic behavior of alpha-chymotrypsin was studied in water-DMSO mixtures at concentrations of the organic solvent that do not cause irreversible denaturation of the enzyme. Various substrates (N-substituted derivatives of L-tyrosine) were found to display substantially different kinetic patterns of interaction with alpha-chymotrypsin, which can be described by totally different kinetic schemes. The differences were ascribed to competition between the N-acyl group of the substrate and the DMSO molecule at the S2-site of substrate binding to the active site of the enzyme.
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Base de dados:
MEDLINE
Assunto principal:
Quimotripsina
/
Dimetil Sulfóxido
Idioma:
Ru
Ano de publicação:
2003
Tipo de documento:
Article