Coenzyme non-specific glutamate dehydrogenase from Chlorella pyrenoidosa 82T: electron microscopic studies

Valery R. Shatilov, Lenina P. Loseva, Vladimir L. Tsuprun, Alla S. Kaftanova, Waclaw L. Kretovich

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)17-20
Number of pages4
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume995
Issue number1
DOIs
StatePublished - Mar 16 1989

Keywords

  • (C. pyrenoidosa)
  • Electron microscopy
  • Glutamate dehydrogenase

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