Characterization of Nla protease from turnip mosaic potyvirus exhibiting a low-temperature optimum catalytic activity.
Kim, D H
Characterization of Nla protease from turnip mosaic potyvirus exhibiting a low-temperature optimum catalytic activity. [electronic resource] - Virology Jul 1996 - 245-9 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0042-6822
10.1006/viro.1996.0372 doi
Amino Acid Sequence
Base Sequence
Binding Sites
Catalysis
DNA, Viral
Endopeptidases--metabolism
Hydrogen-Ion Concentration
Kinetics
Molecular Sequence Data
Potyvirus--enzymology
Protein Conformation
Temperature
Viral Proteins--metabolism
Characterization of Nla protease from turnip mosaic potyvirus exhibiting a low-temperature optimum catalytic activity. [electronic resource] - Virology Jul 1996 - 245-9 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0042-6822
10.1006/viro.1996.0372 doi
Amino Acid Sequence
Base Sequence
Binding Sites
Catalysis
DNA, Viral
Endopeptidases--metabolism
Hydrogen-Ion Concentration
Kinetics
Molecular Sequence Data
Potyvirus--enzymology
Protein Conformation
Temperature
Viral Proteins--metabolism