Journal: Biochemistry and Biophysics Reports
Article Title: Isolation, biochemical characterization, and primary structure and active site determination of Dioscorea opposita (‘Nagaimo’) oligopeptidase B
doi: 10.1016/j.bbrep.2025.102071
Figure Lengend Snippet: Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of serine protease purified from Dioscorea. opposita ‘Nagaimo’. Electrophoresis of the purified protease was performed on a Mini Protean TGX precast gel (any size) in the presence of SDS and the gel was stained with Coomassie Brilliant Blue G-250. Lane 1 contained 2 μg of the purified enzyme in the absence of β-ME, and lane 2 contained the same amount of the protein in the presence of β-ME. Wide-View™ Prestained Protein Size Marker III protein standards (Fuijifilm Wako Pure Chemical Corporation) were used to estimate the molecular weights. The molecular weights of the maker proteins are indicated on the right-hand side.
Article Snippet: Wide-ViewTM prestained protein size marker III (Mr 11–245 kDa), protamine, β-casein, and anti-His-tag antibody (Catalog no. 011–23091) were obtained from FUJIFILM Wako Pure Chemical Co (Osaka, Japan).
Techniques: Polyacrylamide Gel Electrophoresis, SDS Page, Purification, Electrophoresis, Staining, Marker