[Oxidation of p-nitrobenzylamine and p-dimethylaminomethylbenzylamine by amine oxidases from the human placenta and serum]. / Okislenie p-nitrobenzilamina i p-dimetilaminometilbenzilamina aminoksidazami platsenty i syvorotki krovi cheloveka.

Oxidation of p-nitro- and p-dimethylaminomethyl derivatives of benzylamine, catalyzed by amine oxidases from human placenta and blood serum, was studied. The amine oxidase activity was estimated by means of a spectrophotometric procedure involving measurement of aldehyde formed during the reaction after extraction with hexane. For extraction of benzaldehyde and p-nitrobenzaldehyde in the samples HCl was added up to the concentration of 0.17 M and for extraction of p-dimethylaminomethyl benzaldehyde--NaHCO3 up to the 0.5 M concentration. The reaction products were extracted with a yield of 94%, 83% and 78% respectively; molar extinction coefficients for aldehydes at the maximal absorption were equal to 13,080 (241 mn), 16,520 (258 nm), and 11,547 (248 nm), respectively. Analysis of the oxidative reactions using inhibitors Lilly 51,641, deprenyl, aminoguanidine and semicarbazide showed that monoamine oxidase of the A type (95%) and benzylamine oxidase (7%) catalyzed oxidation of 0.1 mM p-nitrobenzylamine in mitochondria and microsomes but oxidation of the substrate at 1 mM concentration was catalyzed by monoamine oxidase of the B type (20% in mitochondria and 35% in microsomes). In the soluble fraction oxidation of p-nitrobenzylamine was catalyzed mainly by diamine oxidase (55%); monoamine oxidase of the A type catalyzed oxidation of 30% of the amine, benzylamine oxidase-15%. The molecular activity of the mitochondrial monoamine oxidase of the A type with p-nitrobenzylamine as a substrate was equal to 61 nmol of the product per 1 mole of the enzyme per 1 min.(ABSTRACT TRUNCATED AT 250 WORDS)

[Modification of the spectrophotometric method of determination of pyridoxal-5'-phosphate and pyridoxal in enzymatic preparations]. / Modifikatsiia spektrofotometricheskogo metoda opredeleniia piridoksal'-5'-fosfata i piridoksalia v fermentnykh preparatakh

In quantitative measurements of pyridoxal-5'-phosphate and pyridoxal in enzymes routinely used phenylhydrasine was substituted for 4-nitrophenylhydrasine. This increased the sensitivity of the method by 70%. The modified procedure had another advantage: it allowed measurements of the optic density of resulting 4-nitrophenylhydrasones at 430 nm for acid solutions and at 550 nm for alkaline solutions.