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- W2110593306 abstract "An aspartic protease that is significantly produced by baculovirus-infected Spodoptera frugiperda Sf9 insect cells was purified to homogeneity from a growth medium. To monitor aspartic protease activity, an internally quenched fluoresce (IQF) substrate specific to cathepsin D was used. The purified aspartic protease showed a single protein band on SDS-PAGE with an apparent molecular mass of 40 kDa. The N-terminal amino acid sequence of the enzyme had a high homology to a Bombyx mori aspartic protease. The enzyme showed greatest affinity for the IQF substrate at pH 3.0 with a K(m) of 0.85 µM. The k(cat) and k(cat)/K(m) values were 13 s(-1) and 15 s(-1) µM(-1) respectively. Pepstatin A proved to be a potent competitive inhibitor with inhibitor constant, K(i), of 25 pM." @default.
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- W2110593306 date "2010-10-23" @default.
- W2110593306 modified "2023-10-17" @default.
- W2110593306 title "Purification and Characterization of Aspartic Protease Derived from Sf9 Insect Cells" @default.
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- W2110593306 doi "https://doi.org/10.1271/bbb.100476" @default.
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