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1 to a reduction of PME48 activity revealed by zymogram.
2 Ps were used to identify MMP activity on the zymogram.
3 protease with a molecular mass of 80 kDa on zymograms.
4 all calpain activity that was detectable on zymograms.
5 the gel and therefore cannot be detected on zymograms.
6 ivity of all the exoprotease species seen in zymograms.
7 le band at 50 kDa predominated in the casein zymograms.
8 apillary whole blood for calibrating gelatin zymograms.
9 03-29, was found to produce a unique band on zymograms (120 kDa) and to react distinctively with a sy
12 ghts of about 57,000 and 47,000 according to zymogram analyses, and the minor xylanases had molecular
25 cription-polymerase chain reaction (RT-PCR), zymograms, and enzyme-linked immunosorbent assay (ELISA)
26 lastidic isoform were detected in vivo using zymograms, and the respective genes were identified usin
27 assay, real-time polymerase chain reaction, zymograms, and Western blot analysis, respectively.We de
28 ity, as assessed by SDS-PAGE and native-PAGE zymogram, appearing as a single band of approximately 22
30 ted SMCs inhibited MMP-2 activity on gelatin zymograms as well as the chemoattractant-directed migrat
31 lytic enzyme, as revealed by its activity in zymograms containing M. luteus cell walls and its abilit
40 e present study aimed to explore the optimal zymogram of exogenous acid protease (ACP), neutral prote
43 s leads to fast and reproducible staining of zymograms permitting reliable quantitation of proteolyti
52 her starch- metabolizing enzymes detected in zymograms, suggest that total DBE catalytic activity is
55 The performances of the predicted optimal zymogram were further verified by in vitro simulated dig