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.
journal_name
Biochimiejournal_title
Biochimieauthors
Cho SW,Lee JEdoi
10.1016/s0300-9084(97)84333-7subject
Has Abstractpub_date
1996-01-01 00:00:00pages
817-21issue
10eissn
0300-9084issn
1638-6183pii
S0300-9084(97)84333-7journal_volume
78pub_type
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