Abstract
The interaction between pig plasma benzylamine oxidase and hydrazine derivatives has been investigated kinetically and spectrophotometrically. The hydrazines tested combine irreversibly to the enzyme and there is a one‐to‐one correspondence between inactivation of the enzyme and hydrazone formation with enzyme‐bound pyridoxal phosphate. Spectrophotometric titration with hydrazines established that benzylamine oxidase contains one mole of reactive pyridoxal phosphate per mole of protein, whereas the copper content is at least two atoms per protein molecule.
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