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

S. W. Cho, J. E. Lee

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)


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
Issue number10
Publication statusPublished - 1996

Bibliographical note

Funding Information:
This work was supported by the Non Directed Research Fund from the Korea Research Foundation ( 1995) and the Asan Institute for Life Sciences (96-04-010) to SW Cho.

All Science Journal Classification (ASJC) codes

  • Biochemistry


Dive into the research topics of 'Modification of brain glutamate dehydrogenase Isoproteins with pyridoxal 5'-phosphate'. Together they form a unique fingerprint.

Cite this