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

FEBS Letters

Jeffery, William A.¹  Watson, Graham J.¹  Thorpe, Philip E.¹  Falasca, Anna¹  Wawrzynczak, Edward J.¹ 

[1] Drug Targeting and Cellular Pharmacology Laboratories, Imperial Cancer Research Fund Laboratories, Lincoln's Inn Fields, London WC2A 3PX, England

关键词: Ricin;    B-chain;    Saccharide binding;    Tyrosine residue;    N-[14C]Acetylimidazole;    RCA;    Ricinus communis agglutinin;    N-AcIm;    N-acetylimidazole;    PBS;    phosphate-buffered saline;    pH 7.2;    HPLC;    high-pressure liquid chromatography;    DMF;    dimethylformamide;    TPCK;    L-(tosylamido-2-phenyl)ethylchloromethylketone;   

DOI  :  10.1016/0014-5793(87)81189-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown