Product Notes
- 7807651 reads
Trypsin from the pyloric caeca of bigeye snapper was purified and characterized. Trypsin had an apparent molecular weight of 23.8 kDa when analyzed using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and substrate-gel electrophoresis. The trypsin fraction consisted of three isoforms as evidenced by the appearance of three different bands on native-PAGE. Optimal activity was observed at 55C and pH range of 8–11.
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