1. Characterization and comparison of recombinant honeybee chymotrypsin-like protease (HCLPase) expressed in Escherichia coli and insect cells.
- Author
-
Matsuoka T, Kawashima T, Nakamura T, and Yabe T
- Subjects
- Amino Acid Sequence, Animals, Baculoviridae genetics, Baculoviridae metabolism, Bees, Cattle, Chymases antagonists & inhibitors, Chymases genetics, Cloning, Molecular, Escherichia coli genetics, Escherichia coli metabolism, Insect Proteins antagonists & inhibitors, Insect Proteins genetics, Kinetics, Leucine chemistry, Oligopeptides chemistry, Phenylalanine chemistry, Protease Inhibitors chemistry, Recombinant Proteins chemistry, Recombinant Proteins genetics, Serum Albumin, Bovine chemistry, Sf9 Cells, Spodoptera, Substrate Specificity, Tyrosine chemistry, Chymases chemistry, Gene Expression, Insect Proteins chemistry, Peptide Fragments chemistry
- Abstract
We previously found a novel chymotrypsin-like protease in honeybee, designated as HCLPase. The recombinant enzyme expressed in insect cells was produced and compared to that in Escherichia coli. Both enzymes showed equivalent molecular size and specificity. However, HCLPase produced in insect cells showed higher specific activity. The C-terminal cleavage sites of HCLPase were phenylalanine, leucine, and tyrosine residues.
- Published
- 2017
- Full Text
- View/download PDF