Abstract
Calf intestinal alkaline phosphatase is inactivated by 2,3-butanedione and phenylglyoxal. The reaction with either reagent results in a biphasic loss of enzymatic activity. Inactivation by 2,3-butanedione in borate buffer can be reversed after gel-filtration in Tris buffer but no enzyme reactivation is observed after phenylglyoxal treatment. Phosphate, ATP and NADH protect the enzyme from both compounds while no protection is displayed by L-phenylalanine. The selective chemical modification indicates that two differently reacting types of arginines are present in the active site domains of the dimeric enzyme.
Lingua originale | English |
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pagine (da-a) | 364-372 |
Numero di pagine | 9 |
Rivista | Italian Journal of Biochemistry |
Volume | 34 |
Stato di pubblicazione | Pubblicato - 1985 |
Keywords
- Alkaline Phosphatase
- Animals
- Arginine
- Binding Sites
- Cattle
- Epoxy Compounds
- Intestines
- Kinetics
- Phenylglyoxal
- Structure-Activity Relationship