Figure 3.

Deglycosylation of the purified β-primeverosidase with glycopeptidase A. The β-primeverosidase purified from tea leaves was mixed in 1% (w/v) Triton X-100 and 50 mm 2-mercaptoethanol, and heated at 100°C for 15 min. The sample was treated with glycopeptidase A in the buffer for 24 h, and was analyzed by 10% (w/v) SDS-PAGE. The protein was visualized by silver staining. The migration of size makers is shown to the left of the gel. Lane 1, β-Primeverosidase purified from tea leaves; lane 2, β-primeverosidase treated with glycopeptidase A.