of midgut proteins from Trichoplusia ni with casein as substrate.
These results con firm that the single band detected by SDS and zymogram
corresponds to trypsin.
Proteolytic activity in zymogram
was visualized, as reported by Garcia-Carreno et al.
2ul of 20 ug recombinant human MMP-2 and 9 standard (Chemicon) as positive control recognized as the standard of MMP-2 and MMP-9 molecular weight were run in each zymogram
The cellulase zymogram
showed six active bands (Cel 1of 74kDa, Cel 2 of 63 kDa, Cel 3 of 62 kDa, Cel 4 of 60 kDa.
oxysporum EMT in the presence of Gallic acid and Guaiacol, and it was investigated using zymogram
analysis on SDS-PAGE.
analysis: For the determination of molecular weight, the enzyme preparations and protein marker (Serva) were subjected to SDS-PAGE.
The protein expression and activity of MMP-9 were determined by Western blot assay and gelatin zymogram
determination of isoenzyme of enzyme produced by B.
of xylanase exhibited a significant activity band that corresponds to result of SDS PAGE.
On the zymogram
two bands were detected, one at a high molecular weight and one at a low weight.
The accuracy/precision of gelatinolytic activities were evaluated by zymogram
densitometry with Image ProPlus software (Cybernetics) (4).