1994 年 58 巻 6 号 p. 1013-1017
A photoactivatable heterobifunctional fluorescent reagent, 1-azido-5-naphthalene sulfonyl (ANS) hydrazide, was synthesized and characterized. ANS-hydrazide reacted with lactose to form a photoactivatable hydrazone. The derivative (ANS-lactose) had the same binding affinity for a conger eel lectin as lactose judging from the hemagglutinating-inhibition assay with rabbit erythrocytes. ANS-lactose was used for photoaffinity labeling of a conger eel lectin. The photolabeled lectin was digested with chymotrypsin to isolate photolabeled peptides by reversed-phase HPLC by monitoring fluorescence. A major labeled peptide was located at positions 31-45 in the lectin by amino acid analysis and N-terminal sequencing. The identified segment was close to the highly conserved region throughout animalβ-galactoside-binding lectins.
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