@article{Kaberdin01082003,
author = {Kaberdin, Vladimir R. and McDowall, Kenneth J.}, 
title = {Expanding the Use of Zymography by the Chemical Linkage of Small, Defined Substrates to the Gel Matrix},
volume = {13}, 
number = {8}, 
pages = {1961-1965}, 
year = {2003}, 
doi = {10.1101/gr.1277303}, 
abstract ={In the postgenomic era, the comprehensive proteomic analysis of metabolic  and signaling pathways is inevitably faced with the challenge of large-scale  identification and characterization of polypeptides with a particular  enzymatic activity. Previous work has shown that a wide variety of enzymatic  activities of microbial, plant, and animal origin can be assigned to  individual polypeptides using in-gel activity staining (zymography). However,  a number of limitations, such as special substrate requirements, the lack of a  standard procedure, and difficulties in distinguishing enzymes with  overlapping activities have precluded the widespread use of zymography as a  routine laboratory method. Here we demonstrate that, by employing  small-defined substrates that are covalently attached to the gel matrix, we  can largely overcome the aforementioned problems and assay readily a number of  different classes of enzymatic activities within gels after standard  SDS-polyacrylamide electrophoresis. Moreover, this development is compatible  with the two-dimensional separation of proteins and thus has great potential  in the high-throughput screening and characterization of complex biological  and clinical samples.}, 
URL = {http://genome.cshlp.org/content/13/8/1961.abstract}, 
eprint = {http://genome.cshlp.org/content/13/8/1961.full.pdf+html}, 
journal = {Genome Research} 
}