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- noun biochemistry A form of
electrophoresisused in the study of enzymeactivity
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Secretion of MMP-2 was evaluated by gelatin zymography, as previously described (Barille et al. 1999).
HA, s-GAG and MMP-2 releases to media were measured using ELISA, dye-binding assay and gelatin zymography, respectively.
Hypoxia increased gelatinolytic activity specifically in vascular structures and gel zymography identified MMP-9 as enzymatic source.
The expression and activity of matrix metalloproteinase 2 (MMP-2) within the tumor were determined by immunohistochemitry and zymography.
Western blot shows tPA protein level (a) and zymography shows tPA activity (b) in MCAo mice with or without MSC treatment. tPA and PAI-1 expression was significantly increased in the IBZ of mice subjected to MCAo compared with normal mice. tPA expression was significantly increased and PAI-1 expression was significantly decreased in the IBZ of MCAo mice after MSC treatment compared with MCAo alone mice (c).
In this regard, this activated form could be detected by zymography in supernatants of all melanoma cell lines that cross-presented the
Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS / PAGE) zymography was performed for determination of gelatinase activity as described before
The proteolytic activity of MMP-9 measured by zymography was also significantly diminished in mice treated daily with i.p. injections of minocycline and i.v. injections of PEG minocycline-liposomes every five days (B).
Proteolytic activity of MMP-9 was assessed in supernatants of human PBMCs after 24 hrs of stimulation with IL-2 and assessed by gelatin-zymography, as previously described
Gelatinolytic activity was detectable by gelatin-zymography at molecular weights of 92 kDa, indicative of MMP-9, in the supernatants from all human PBMC samples studied.
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