Modification of brain glutamate dehydrogenase Isoproteins with pyridoxal 5'-phosphate

S. W. Cho, Jongeun Lee

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Two soluble forms of brain glutamate dehydrogenase isoproteins were inactivated by pyridoxal 5'-phosphate. Restoration of catalytic activity can be accomplished by dialysis and addition of an excess of cysteine or lysine. Spectral evidence is presented to indicate that the inactivation proceeds through Schiff base formation with amino groups of the enzyme. Inactivation became irreversible after reduction with NaBH4 and the NaBH4-reduced enzyme showed a characteristic absorption peak at 325 nm. Using spectral titration at 325 nm, the stoichiometry was 2 mol/mol of GDH subunit without protection and 1 mol/mol with protection, indicating the complete masking of one mol of lysine. The results with analogs of pyridoxal 5'-phosphate show that the aldehyde group, but not the phosphate group, is required for efficient inactivation.

Original languageEnglish
Pages (from-to)817-821
Number of pages5
JournalBiochimie
Volume78
Issue number10
DOIs
Publication statusPublished - 1996 Jan 1

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Glutamate Dehydrogenase
Pyridoxal Phosphate
Lysine
Brain
Dialysis
Schiff Bases
Enzymes
Titration
Aldehydes
Stoichiometry
Restoration
Cysteine
Catalyst activity
Phosphates

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

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Modification of brain glutamate dehydrogenase Isoproteins with pyridoxal 5'-phosphate. / Cho, S. W.; Lee, Jongeun.

In: Biochimie, Vol. 78, No. 10, 01.01.1996, p. 817-821.

Research output: Contribution to journalArticle

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