Isolation and sequencing of an active-site peptide from spinach ferredoxin-NADP + oxidoreductase after affinity labeling with periodate-oxidized NADP

Spinach ferredoxin-NADP + oxidoreductase was inactivated by treatment with 2′,3′-dialdehyde NADP + (periodate-oxidized NADP +), which selectively modifies a lysine residue at the nucleotide-binding domain of the enzyme. The identity of the derivatized residue was ascertained by thin-layer chromatogr...

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Veröffentlicht in:	Archives of biochemistry and biophysics 1985-07, Vol.240 (1), p.172-177
Hauptverfasser:	Chan, Raquel L., Carrillo, Nestor, Vallejos, Rubén H.
Format:	Artikel
Sprache:	eng
Schlagworte:	Affinity Labels Amino Acid Sequence Amino Acids - isolation & purification Applied sciences Binding Sites Chromatography, High Pressure Liquid Exact sciences and technology Ferredoxin-NADP Reductase - metabolism NADH, NADPH Oxidoreductases - metabolism NADP - analogs & derivatives Other techniques and industries Oxidation-Reduction Peptide Fragments - isolation & purification Plants - enzymology
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