Apr 1, 1976

Human saliva peroxidase: microanalytical isoelectric fractionation and properties in normal persons and in cases with neuronal ceroid-lipofuscinosis

Clinical Biochemistry
H PilzR Heipertz

Abstract

Human saliva contains a high peroxidase activity that can be estimated spectrophotometrically with the hydrogen donor p-phenylenediamine and the substrate hydrogen peroxide from 20 mul of material. The pH optimum of the enzyme with citrate-phosphate buffer is 5.5. After microanalytical isoelectric fractionation 3 main isoenzyme components at pI 8.6, 6.5 and 4.3, and a number of isoenzyme subfractions at pI 9.5, 7.3 and 3.8 are detectable. In 3 patients with the juvenile form of neuronal ceroid-lipofuscinosis (type Spielmeyer-Vogt), in which a deficiency of leukocyte peroxidase had been reported by other authors, both the total activity of saliva peroxidase and the activity of individual isoenzymes were found to be within normal limits. These findings are not consistent with a generalized peroxidase deficiency in this disease.

  • References1
  • Citations7

References

  • References1
  • Citations7

Citations

Mentioned in this Paper

Ovoperoxidase
Inborn Errors of Metabolism
Ceroid
Phosphate buffers
Hydrogen Peroxide
Peroxidases
Saliva - SpecimenType
Peroxidase Activity
Citrate Measurement
Lipofuscin

About this Paper

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