Studies on the selective chemical inhibition by urea of alkaline phosphatase isoenzymes in the reaction course

Alvaro Mordente, Elisabetta Meucci, Ga Miggiano, M Pileri, Ge Martorana, A. Castelli

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Urea inhibits the activity of alkaline phosphatase during the reaction course. The inactivation is progressively stronger for the placental, intestinal and renal subforms. Influence of reaction temperature, pH, type and molarity of buffer, magnesium chloride, albumin and enzyme concentration on the inactivation mechanism is evaluated. In all experimental conditions the process follows pseudofirst-order kinetics and the inactivation profiles are distinct and typical for each enzymatic subform. With a simple graphical analysis, a single inactivation curve in controlled experimental conditions, allows the identification of each isoenzyme from the slope and the calculation of the respective fractional amount from the intercept of the time-activity plot.
Original languageEnglish
Pages (from-to)162-169
Number of pages8
JournalENZYME
Volume32
Publication statusPublished - 1984

Keywords

  • Alkaline Phosphatase
  • Animals
  • Buffers
  • Cattle
  • Female
  • Humans
  • Hydrogen-Ion Concentration
  • Isoenzymes
  • Kinetics
  • Magnesium
  • Magnesium Chloride
  • Pregnancy
  • Urea

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