Modification of arginine residues in calf intestinal alkaline phosphatase

Alvaro Mordente, Ga Miggiano, Ge Martorana, A. Castelli

Risultato della ricerca: Contributo in rivistaArticolo in rivista

2 Citazioni (Scopus)

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 originaleEnglish
pagine (da-a)364-372
Numero di pagine9
RivistaItalian Journal of Biochemistry
Volume34
Stato di pubblicazionePubblicato - 1985

Keywords

  • Alkaline Phosphatase
  • Animals
  • Arginine
  • Binding Sites
  • Cattle
  • Epoxy Compounds
  • Intestines
  • Kinetics
  • Phenylglyoxal
  • Structure-Activity Relationship

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