From owner-cellbiol@net.bio.net Mon Feb 03 22:00:00 1997 Path: biosci!rutgers!gatech!csulb.edu!hammer.uoregon.edu!arclight.uoregon.edu!hunter.premier.net!news.maxwell.syr.edu!cpk-news-hub1.bbnplanet.com!news.bbnplanet.com!su-news-hub1.bbnplanet.com!newsxfer3.itd.umich.edu!howland.erols.net!rill.news.pipex.net!pipex!warwick!leicester!usenet From: "Dr E. Buxbaum" Newsgroups: bionet.cellbiol Subject: Re: glycosylation Date: 4 Feb 1997 17:40:41 GMT Organization: University of Leicester, UK (PCFS User) Lines: 13 Message-ID: <5d7sap$9c9@falcon.le.ac.uk> References: <199702032102.QAA19223@pilot19.cl.msu.edu> NNTP-Posting-Host: pc47.msb.le.ac.uk Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 1.22 (Windows; I; 16bit) delgadoi@PILOT.MSU.EDU ("Ivan J Delgado") wrote: > > A question regarding glycosylation of proteins and how that looks in > a western. Glycosylation leads to spread out, unsharp bands in SDS-PAGE (and consequentially in Westerns), which have a higher molecular weight than the unglycosylated protein. A nice way to check for glycosylation is to stain the gel or the western blot with Feulgen's reagent. Gives bright red bands, a very beautifull color. .