Andrzej Szutowicz

TL;DR: Kinetic parameters of liver and brain monoamine oxidase with various substrates and inhibitors appeared to be the same when determined by either colorimetric or radiometric methods.

TL;DR: The data indicate that the differential regulation of ATP‐citrate lyase activity in cholinergic and adrenergic cells does not result from the existence of different molecular forms of the enzyme in these cell lines, and provide further evidence to support the hypothesis that ATP‐ citrate Lyase activity increases during maturation of normal cholinerential neurons and decreases in noncholinergic cells of the brain.

TL;DR: The activities of choline acetyltransferase and ATP‐citrate lyase were significantly correlated (r = 0.995) in fractions of small and large synaptosomes isolated from rat hippocampus and cerebellum, providing additional evidence linking ATP‐ citrate Lyase to the cholinergic system in the brain.

TL;DR: Monoamine oxidase B has been purified from human blood platelets 185-fold to a specific activity of 113 nmole/min/mg protein by a combination of Triton X-100 solubilization and ion exchange chromatography.

TL;DR: Data indicate that rat brain ATP-citrate lyase is similar or identical to that present in rat liver, which has the same electrophoretic mobility, as well as the same immunoreactivity against specific rabbit anti-rat liver ATP- citrate Lyase antibody.