Treatment of normal human brain mitochondria with a mixture containing Triton X-100 and urea resulted in solubilization of monoamine oxidase (MAO) exhibiting tyramine-, serotonine-, phenylethylamine- and dopamine deaminase activities at ratios similar to those characteristic for the initial mitochondria. A purified preparation of the enzyme was obtained after AH-Sepharose chromatography; it was shown that in the brain there were present four isoenzymes of MAO possessing different substrate specificity. Investigation of some properties of MAO (activity, solubilization and isozyme composition) from brain regions showed absence of asymmetry and higher enzymatic activity in the subcortical brain region as compared with right and left brain cortex.
Kamyshanskaia N.S., Moskvitina T.A. (1981) Multiple forms of human brain monoamine oxidase. Voprosy Meditsinskoi Khimii, 27(2), 261-266.
Kamyshanskaia N.S. et al. Multiple forms of human brain monoamine oxidase // Voprosy Meditsinskoi Khimii. - 1981. - V. 27. -N 2. - P. 261-266.
Kamyshanskaia N.S. et al., "Multiple forms of human brain monoamine oxidase." Voprosy Meditsinskoi Khimii 27.2 (1981): 261-266.
Kamyshanskaia, N. S., Moskvitina, T. A. (1981). Multiple forms of human brain monoamine oxidase. Voprosy Meditsinskoi Khimii, 27(2), 261-266.