Biochemical studies on ricin. XII. Iodination of ricin D.

Ishiguro, Masatsune; Taira, Etsuko; Mashima, Kazuto; Funatsu, Gunki; Funatsu, Masaru; Kikutani, Motosuke

doi:10.1271/bbb1961.41.299

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Identification of a tyrosine residue in the saccharide binding site of ricin B‐chain using N‐[¹⁴C]acetylimidazole

et al. 1987

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The binding of ricin B-chain to Sepharose, a galactose-based adsorbent, was reversibly inactivated by acetylation of tyrosine residues in the absence of lactose. In the presence of lactose, two tyrosine residues were protected against modification and the B-chain retained its binding ability. Analyses of tryptic peptides from B-chain modified with N-[14C]acetylimidazole in the presence and absence of lactose showed that Tyr-248 is present in one of the galactose-binding sites.

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