Brain Peroxidase and Catalase in Parkinson Disease
- 1 February 1975
- journal article
- research article
- Published by American Medical Association (AMA) in Archives of Neurology
- Vol. 32 (2) , 114-118
- https://doi.org/10.1001/archneur.1975.00490440064010
Abstract
Peroxidase and catalase activities were determined in various regions of parkinsonian brains and control brains from patients with nonneurological diseases. The highest peroxidase activity was localized in the substantia nigra of the normal brain. In Parkinson disease, the peroxidase activity was decreased in the substantia nigra, caudate, and putamen. Catalase activity was also reduced in the substantia nigra and putamen of the parkinsonian brain. These enzyme changes may be causally related to the degeneration and depigmentation of the substantia nigra neurons in Parkinson disease.Keywords
This publication has 13 references indexed in Scilit:
- In vivo generation of hydrogen peroxide from 6-hydroxydopamineCellular and Molecular Life Sciences, 1972
- Tyrosine hydroxylase in rat brain—cofactor requirements, regional and subcellular distributionBiochemical Pharmacology, 1972
- The role of peroxidase in catalyzing oxidation of polyphenolsBiochimica et Biophysica Acta (BBA) - General Subjects, 1971
- Inhibition of Biogenic Amine Uptake by Hydrogen Peroxide: A Mechanism for Toxic Effects of 6-HydroxydopamineScience, 1971
- Sensitive method for determination of peroxidase activity in tissue by means of coupled oxidation reactionAnalytical Biochemistry, 1971
- Possible Etiology of Schizophrenia: Progressive Damage to the Noradrenergic Reward System by 6-HydroxydopamineScience, 1971
- A method for assay of catalase with the oxygen cathodeAnalytical Biochemistry, 1968
- Hydroxylation: the activation of oxygen by peroxidaseBiochimica et Biophysica Acta, 1957
- The action of peroxidase with enzymically generated peroxide in the presence of catalaseBiochimica et Biophysica Acta, 1954
- Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobinBiochemical Journal, 1951