Involvement of arginine residues in inhibition of protein synthesis by ricin A‐chain

FEBS Letters

Funatsu, Gunki¹  Watanabe, Keiichi¹ 

[1]Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka 812, Japan

关键词: Ricin A-chain Ribosome inactivation Active site Arginine residue;    PGO;    phenylglyoxal;    CHD;    1;    2-cyclohexanedione;    HPLC;    high-performance liquid chromatography;   

DOI  :  10.1016/0014-5793(86)80815-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Modifications of arginine residues in ricin A-chain with phenylglyoxal (PGO) and 1,2-cyclohexanedione (CHD) caused a marked loss in its inhibitory activity on cell-free protein synthesis. The loss of activity caused by modification with PGO was much faster than the loss of total arginine residues. More than 90% activity was lost with PGO modification of about three arginine residues. Regeneration of arginine residues from the CHD-modified residues resulted in complete recovery of the activity. These results strongly suggest the involvement of definite arginine residue(s) in A-chain activity. Analysis of the peptides, produced by peptic digestion of the [¹⁴C]PGO-modified A-chain, showed that some of the six arginine residues in the N-terminal region of A-chain react with PGO faster than other arginine residues.

【 授权许可】

Unknown