Effects on Enzyme Activity of Ligand-Binding to Copper in Pig-Plasma Benzylamine Oxidase

Active-sitve titration of pig plasma benzylamine oxidase with phenylhydrazine.

Pig plasma benzylamine oxidase is a protein containing cupric copper and pyridoxal phosphate. The pyridoxal phosphate is stably linked to the enzyme. Discrepancies in the numbers of active sites per molecule of enzyme are reported in the literature. This paper shows that the fully active pure enzyme contains 3 mol of pyridoxal phosphate per mol, whereas enzymes with a lower specific activity ar...

High affinity lipid binding sites on the peripheral membrane enzyme pyruvate oxidase. Specific ligand effects on detergent binding.

Pyruvate oxidase is a peripheral membrane enzyme which has been purified to homogeneity from Escherichia coli. When assayed in the presence of some amphiphiles the enzymatic activity is stimulated nearly 25fold; these amphiphiles include phospholipids, neutral detergents, and charged detergents. Both anionic and cationic detergents, at concentrations well below their critical micelle concentrat...

Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methods.

Benzylamine oxidase from pig plasma has been studied by a variety of chemical and physical techniques. 1. Analytical ultracentrifugation, gel electrophoresis and isoelectric-focusing studies suggest that the enzyme is composed of two subunits with closely similar primary structures. 2. E.s.r. and n.m.r. measurements show that the enzyme contains two well-separated (greater than 0.6 nm) Cu2+ ion...

evaluation of systemic effects of ginger fractions on salivation in rats

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optimization of bacterial urate oxidase enzyme activity