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百日咳毒素形成的ADP-核糖基化蛋白可被汞离子特异性切割。

ADP-ribosyl proteins formed by pertussis toxin are specifically cleaved by mercury ions.

作者信息

Meyer T, Koch R, Fanick W, Hilz H

机构信息

Institut für Physiologische Chemie, Universität Hamburg, Germany.

出版信息

Biol Chem Hoppe Seyler. 1988 Jul;369(7):579-83. doi: 10.1515/bchm3.1988.369.2.579.

DOI:10.1515/bchm3.1988.369.2.579
PMID:3223989
Abstract

Various types of ADP-ribosyl protein conjugates were synthesized and their chemical stability was compared with that of cysteine-linked ADP-ribosyl groups as formed by incubation of transducin or Gi/Go proteins with NAD and pertussis toxin. Treatment with 0.1 mM HgCl2 specifically cleaved the cysteine-linked conjugates. This may provide a tool for the quantitation of modified Gi/Go proteins as well as of other acceptors modified by ADP-ribose at cysteine residues in the presence of other ADP-ribosyl proteins.

摘要

合成了各种类型的ADP-核糖基化蛋白质缀合物,并将其化学稳定性与通过转导素或Gi/Go蛋白与NAD和百日咳毒素孵育形成的半胱氨酸连接的ADP-核糖基团的化学稳定性进行了比较。用0.1 mM HgCl2处理可特异性切割半胱氨酸连接的缀合物。这可能为在存在其他ADP-核糖基化蛋白质的情况下,定量修饰的Gi/Go蛋白以及在半胱氨酸残基处被ADP-核糖修饰的其他受体提供一种工具。

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