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Polymorphic glutamate dehydrogenase in lilac vitroplants as revealed by combined preparative IEF and native PAGE: Effect of ammonium deprivation, darkness and atmospheric CO 2 enrichment upon isomerization
Author(s) -
Refouvelet Eric,
Daguin Florence
Publication year - 1999
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1034/j.1399-3054.1999.105203.x
Subject(s) - ammonium , chemistry , isoelectric focusing , glutamate dehydrogenase , lilac , chromatography , enzyme , biochemistry , biology , botany , glutamate receptor , organic chemistry , receptor
The activity and polymorphism of glutamate dehydrogenase (GDH) were studied in basal callus of lilac ( Syringa vulgaris L.) vitroplants. Native PAGE alone revealed seven bands staggered at regular intervals. Preparative liquid‐vein IEF allowed the separation of six to ten GDH fractions with charges ranging between 5.18 and 7.08. Analysis of these GDH fractions in native PAGE indicated that up to seven GDH bands can be detected for each fraction. This suggests the existence of seven isoforms of the enzyme with subunits presenting different isoelectric points. Dark‐ and ammonium‐controlled forms were found to be the more acidic and faster migrating ones in native PAGE. The results support for the first time that atmospheric CO 2 enrichment increases GDH activity dramatically and modifies isomerization of the enzyme.