Coenzyme non-specific glutamate dehydrogenase from Chlorella pyrenoidosa 82T: electron microscopic studies.
The constitutive coenzyme non-specific glutamate dehydrogenase (GDH) from Chlorella pyrenoidosa 82T was purified to homogeneity by column immunoaffinity chromatography and examined by an electron microscope. The enzyme molecule was found to be a hexameric oligomer composed of monomers arranged in three 2-point group symmetry in two layers slightly twisted round the 3-fold axis. The molecule is 8 +/- 1 nm in diameter and 10 +/- 1 nm in height. The enzyme molecules appear both to dissociate into trimers and to associate along the 3-fold axis forming linear aggregates under certain conditions. A tentative model of the Chlorella GDH molecule is proposed, which is very similar to those described for bovine liver GDH and GDH from Clostridium symbiosum.
Shatilov
V R
VR
A.N. Bach Institute of Biochemistry, U.S.S.R. Academy of Sciences, Moscow.
Loseva
L P
LP
Tsuprun
V L
VL
Kaftanova
A S
AS
Kretovich
W L
WL
D002708:Chlorella / Q000201:enzymology*; D005969:Glutamate Dehydrogenase; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D015394:Molecular Structure
D046911:Macromolecular Substances; D005969:Glutamate Dehydrogenase