Youssef Farhat, Written 4/8/13, Last Updated 5/10/13
Here, we summarize possible ways of interpreting individual bands that can be visualized on gelatin zymography based on their molecular weight. These interpretations have been reported in the papers cited below. Note that these interpretations need further confirmation with techniques such as Western blots or cutting out the bands and sending them off for sequencing by a proteomics center (let me know if you are aware of other ways to identify them by sending an email to youssef@protocol-place.com).
| Molecular Weight (kDa) | Possible Interpretation |
| 240 |
|
| 215 |
|
| ~200 |
|
| 180 |
|
| ~140-144 |
|
| 125 |
|
| 92 |
|
| 83-85 | |
| 82 |
|
| 72 |
|
| 67-68 | |
| 64 |
|
| 62 |
|
| 58 |
|
| 57 |
|
| 55 |
|
| 45 | |
| 43 |
|
| 28 |
|
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References
1. Snoek-van Beurden, P.A. and J.W. Von den Hoff, Zymographic techniques for the analysis of matrix metalloproteinases and their inhibitors. Biotechniques, 2005. 38(1): p. 73-83.
2. Toth, M. and R. Fridman, Assessment of Gelatinases (MMP-2 and MMP-9 by Gelatin Zymography. Methods in molecular medicine, 2001. 57: p. 163-74.
3. Koo, B.H., et al., Dimerization of matrix metalloproteinase-2 (MMP-2): functional implication in MMP-2 activation. J Biol Chem, 2012. 287(27): p. 22643-53.
4. Troeberg, L. and H. Nagase, Measurement of matrix metalloproteinase activities in the medium of cultured synoviocytes using zymography. Methods Mol Biol, 2003. 225: p. 77-87.
5. Hussain, A.A., Y. Lee, and J. Marshall, High molecular-weight gelatinase species of human Bruch’s membrane: compositional analyses and age-related changes. Investigative ophthalmology & visual science, 2010. 51(5): p. 2363-71.
