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.
|Numero di pagine||9|
|Rivista||Italian Journal of Biochemistry|
|Stato di pubblicazione||Pubblicato - 1985|
- Alkaline Phosphatase
- Binding Sites
- Epoxy Compounds
- Structure-Activity Relationship