A mutationally altered alkaline phosphatase from Escherichia coli. II. Structural and catalytic properties of the activated enzyme. [electronic resource]
- The Journal of biological chemistry Apr 1972
- 2095-101 p. digital
Publication Type: Journal Article
0021-9258
Alkaline Phosphatase Amino Acids Catalysis Chemical Phenomena Chemistry Circular Dichroism Drug Stability Enzyme Activation Escherichia coli--enzymology Hot Temperature Hydrogen-Ion Concentration Kinetics Mathematics Mutation Nitrophenols Optical Rotatory Dispersion Phosphoric Acids Protein Conformation Species Specificity Spectrophotometry Ultracentrifugation