A mutationally altered alkaline phosphatase from Escherichia coli. II. Structural and catalytic properties of the activated enzyme. [electronic resource]
Producer: 19720615Description: 2095-101 p. digitalISSN:- 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
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Publication Type: Journal Article
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