|
Sci. STKE, 12 June 2001 PROTOCOLSThe Biotin Switch Method for the Detection of S-Nitrosylated ProteinsSamie R. Jaffrey, and Solomon H. Snyder The authors are in the Departments of Neuroscience, Pharmacology and Molecular Sciences, and Psychiatry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. E-mail: jaffrey{at}jhmi.edu; ssnyder {at}jhmi.edu Abstract: Many of the effects of nitric oxide are mediated by the direct modification of cysteine residues resulting in an adduct called a nitrosothiol. Here, we describe a novel method for detecting proteins that contain nitrosothiols. In this three-step procedure, nitrosylated cysteines are converted to biotinylated cysteines. Biotinylated proteins can then be detected by immunoblotting or can be purified by avidin-affinity chromatography. We include examples of the detection of S-nitrosylated proteins in brain lysates after in vitro S-nitrosylation, as well as the detection of endogenous S-nitrosothiols in selected neuronal proteins. Citation: © 2001 American Association for the Advancement of Science
Citation: S. R. Jaffrey, S. H. Snyder, The Biotin Switch Method for the Detection of S-Nitrosylated Proteins. Sci. STKE 2001, pl1 (2001). The editors suggest the following Related Resources on Science sites:In Science Signaling
|
Science Signaling. ISSN 1937-9145 (pre-2008: Science's STKE. ISSN 1525-8882)
Magazine | News | Signaling | Careers | Multimedia | Collections | Help | Site Map | RSS
Subscribe | Feedback | Privacy / Legal | About Us | Advertise With Us | Contact Us
© 2001 American Association for the Advancement of Science. All Rights Reserved.
AAAS is a partner of HINARI, AGORA, PatientInform, CrossRef, and COUNTER.
You have reached the bottom of the page. Back to top