Location of cysteine residues and the biological activities of the fluorescence-labeled cinnamomin

被引：0
作者：
Xie, L
Hou, FJ
Liu, WY
Wang, ED
机构：
[1] Acad Sinica, Shanghai Inst Biochem, Lab Ribosome Res, Shanghai 200031, Peoples R China
[2] Acad Sinica, Shanghai Inst Biochem, State Key Lab Mol Biol, Shanghai 200031, Peoples R China
来源：
PROTEIN AND PEPTIDE LETTERS | 2000年 / 7卷 / 04期
关键词：
cinnamomin; ribosome-inactivating protein; SH groups; sugar chain; titration;
D O I：
暂无
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Cinnamomin is a type II ribosome-inactivating protein (RIP) isolated from the seeds of Cinnamomum camphora. It is composed of two glycopeptide chains (A- and B-chain). The A-chain exhibits RNA N-glycosidase activity, depurinating an adenosine from the largest ribosomal RNA and thus inhibiting protein synthesis, The B-chain is a lectin, recognizing the galactose-containing receptor on the cell surface and facilitating entry of the A-chain into the cell. A total of ten cysteines were titrated with DTNB in the cinnamomin molecule, one in the A-chain and the other in the B-chain. All the cysteines existed in the disulfide bond form in cinnamomin, which probably accounted for its high structural stability. On the other hand, the sugar chains of cinnamomin were oxidized with periodate and then fluorescence-labeled with FTSC. Both the RNA N-glycosidase activity of its A-chain and the lectin activity of its B-chain decreased three fold after fluorescence-labeling.
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页码：265 / 272
页数：8
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