卵白 Flavoprotein の化学修飾(生活科学)

概要

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Flavin-binding capacity of chicken egg white apoprotein and its chemically modified derivatives were investigated. No major change was observed in the flavin-binding capacity of acetylated, succinylated and carbamylated apoprotein as compared with that of native apoprotein. The flavin-binding capacity of apoprotein was destroyed by reduction, S-carboxymethylation, iodination and modification of tryptophane residue with Koshland's reagent. 8 M-Urea treatment also inhibits the flavin-binding but this inhibition was reversed after dialysis. We conclude from the experiments described above that the flavin-binding site of apoprotein are tryptophane or histidine residue. The binding site requires tertiary structure which is supported by hydrogen bond and is stabilized by disulfide bond of the peptide chain.
京都府立大学の論文
1973-10-31