Staining of concanavalin a reactive glyco proteins on poly acrylamide gels with horseradish peroxidase a critical evaluation

Schott K J.; Neuhoff, V.; Nessel, B.; Poetter, U.; Schroeter, J.

Electrophoresis 5(2): 77-83

1984


ISSN/ISBN: 0173-0835
DOI: 10.1002/elps.1150050204
Accession: 006471736

Download citation:  
Text
  |  
BibTeX
  |  
RIS

Article/Abstract emailed within 0-6 h
Payments are secure & encrypted
Powered by Stripe
Powered by PayPal

Abstract
The method to localize and quantitate glycoproteins on polyacrylamide gels is based on the binding of concanavalin A to the glycoproteins and the subsequent coupling of horseradish peroxidase to the glycoprotein.sbd.concanavalin A complex. The complex is visualized by the oxidation of 3,3'-diaminobenzidine with horseradish peroxidase-H2O2, forming a brownish stain at the gel surface. Various parameters are analyzed and a scheme for the optimal staining of macro and micro slab gels is given. The quantitative evaluation of the stained gels is demonstrated. The staining and quantitation of nitrocellulose transfers is also shown.

Staining of concanavalin a reactive glyco proteins on poly acrylamide gels with horseradish peroxidase a critical evaluation