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MMP-2 protein secretion and activation in the culture supernatants were measured using gelatin zymography under non-reducing conditions as described previously [41].
MMP activity was measured using gelatin zymography.
Plasma MMPs were measured using gelatin zymography as described by Sepper et al. [ 23].
MMPs in conditioned media (B ) and cell lysates (C ) were measured using gelatin zymography.
MMPs in conditioned media (A ) and cell lysates (B ) were measured using gelatin zymography.
MMP-2 and MMP-9 expression in synovial explants and HMVEC supernatants were measured using gelatin zymography (6 mg/ml).
Similar(51)
Gelatinolytic activity of serum MMP-2 and MMP-9 was measured using the gelatin zymography technique.
Gelatinase activity was measured using the gelatin-zymography assay, and its inhibition showed that three hydroxyl groups at the A or B ring, or, for non-planar molecules, a galloyl moiety at C3 could be determinant.
Matrix metalloproteinase (MMP -2 and MMP -2andivities were measured using a type I gelatin zymography technique.
The tensile properties such as tensile strength (TS), tensile modulus (TM) and elongation at break (Eb %) of the scaffolds of γ-ray-irradiated and non-irradiated gelatin were measured using a universal testing machine (model: H50KS-0404, HounSeries Series S, UK) with 5,000 N load range at a crosshead speed of 20 mm/min.
HA, s-GAG and MMP-2 releases to media were measured using ELISA, dye-binding assay and gelatin zymography, respectively.
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