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- W2017670099 abstract "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 chromatography of the protein hydrolysate. Reductase that had been labeled with periodate-oxidized NADP+ and NaB3H4 was treated with trypsin, and samples of the tryptic digest were subjected to reverse-phase high-performance liquid chromatography. The radioactivity profiles showed modification of one specific peptide. The primary structure of this peptide was found to be Gly-Glu-Lys∗-Met-Tyr-Ile-Gln-Thr-Arg, where Lys∗ represents the derivatized lysine. The sequence obtained corresponds to residues 242–250 in the primary structure of spinach ferredoxin-NADP+ reductase recently reported [Karplus et al. (1984) Biochemistry23, 6576–6583]." @default.
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- W2017670099 title "Isolation and sequencing of an active-site peptide from spinach ferredoxin-NADP+ oxidoreductase after affinity labeling with periodate-oxidized NADP+" @default.
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- W2017670099 doi "https://doi.org/10.1016/0003-9861(85)90020-7" @default.
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