[Preparation and properties of isocitrate lyase isoforms from the cotyledons of Glycine max L].
Prikl Biokhim Mikrobiol
; 46(1): 103-8, 2010.
Article
en Ru
| MEDLINE
| ID: mdl-20198926
ABSTRACT
A four-stage purification procedure including ammonium sulfate precipitation and ion exchange chromatography on DEAE cellulose has been elaborated for isolation of isocitrate lyase (EC 4.1.3.1) isoforms from the cotyledons of soybean Glycine max L. Electrophoretically homogeneous preparations of two forms of the enzyme with specific activity of 5.28 and 5.81 U/mg protein have been obtained. Comparison of physicochemical, kinetic, and regulation characteristics of the isoforms obtained revealed fundamental differences between them. Thus, the isoform that migrated quickly in PAAG had a much lower affinity to isocitrate (K(M) - 50 microM) than the slowly migrating form (K(M) - 16 microM). It has been shown that the conservation of activity of the isoforms obtained depends on the presence of divalent cations (Mn2+ and Mg2+) in the medium. It is suggested to use the isoforms of isocitrate lyase isolated from soybeans for the development of biosensors for biochemical and kinetic assays.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas de Plantas
/
Glycine max
/
Cotiledón
/
Isocitratoliasa
Idioma:
Ru
Revista:
Prikl Biokhim Mikrobiol
Año:
2010
Tipo del documento:
Article