1. Academic Validation
  2. X-Prolyl dipeptidyl-aminopeptidase activity, with X-proline p-nitroanilides as substrates, in normal and pathological human sera

X-Prolyl dipeptidyl-aminopeptidase activity, with X-proline p-nitroanilides as substrates, in normal and pathological human sera

  • Clin Chem. 1976 Aug;22(8):1256-61.
M Hino H Fuyamada T Hayakawa T Nagatsu H Oya
PMID: 949833
Abstract

X-Prolyl dipeptidyl-aminopeptidase (no EC no. assigned) activity in normal and pathological human sera was assayed with several newly synthesized X-proline p-nitroanilides as chromogenic substrates. Normal values for 88 healthy subjects (15 to 81 years old), with glycylproline p-nitroanilide as substrate at pH 8.7, were 54.9 +/- 1.5 (SE) (range, 25.7 - 96.0) mumol/min per liter of serum at 37 degrees C. The results suggest that the Enzyme activities with all X-proline p-nitroanilides were increased in patients with hepatitis and decreased in patients with gastric Cancer. On Sephadex G-200 column chromatography, normal human sera showed a single peak of Enzyme activity with glycylproline p-nitroanilide as the substrate, which coincided with the peak with glycylproline beta-naphthylamide but was different from the peaks with leucine beta-naphthylamide. Sera from patients with hepatitis or liver cirrhosis showed an increase in the normal peak and the appearance of another new peak with glycylproline p-nitroanilide as substrate.

Figures
Products
  • Cat. No.
    Product Name
    Description
    Target
    Research Area
  • HY-16710
    99.99%, Dipeptidyl Peptidase IV Substrate