Isolation of an active site peptide from spinach ribulose bisphosphate carboxylase/oxygenase modified by glyoxylate
Conference
·
OSTI ID:5745272
Gloxylate has been shown to be a slowly reversible inhibitor of CO/sub 2//Mg/sup 2 +/-activated ribulose-P/sub 2/ carboxylase/oxygenase. Reduction of the glyoxylate-enzyme complex with sodium borohydride resulted in a convalently modified adduct indicative of Schiff base formation between glyoxylate and the epsilon-NH/sub 2/ gorup of lysyl residues. Complete inactivation of the enzyme corresponded to the incorporation of 1 mol glyoxylate/mol protomer (L + S subunit). The formation of a covalently modified glyoxylate-enzyme complex has enabled the purification and sequencing of the glyoxylate-derivitized peptide and identification of the amino acid bearing the glyoxylate moiety.
- Research Organization:
- Union Carbide Corp., Oak Ridge, TN (USA). Nuclear Div.
- DOE Contract Number:
- W-7405-ENG-26
- OSTI ID:
- 5745272
- Report Number(s):
- CONF-8308110-1; ON: DE83017219
- Country of Publication:
- United States
- Language:
- English
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