Allicin was prepared daily for our animal studies by reacting alliin and alliinase. Alliin was produced by a modified method developed by Stoll and Seebeck. The chemical and spectral properties of the synthetic alliin were identical to those of the natural product in the garlic clove. Alliinase extraction and purification were performed as described previously. The enzymatic activity of alliinase and the rate of production of allicin and pyruvate were determined by spectrophotometry in a coupled reaction which uses reduced nicotinamide adenine dinucleotide and lactic dehydrogenase to generate nicotinamide dinucleotide and lactic acid. The allicin was prepared just before administration by interaction of alliin (10 mg/kg rabbit) with purified alliinase (3 U/mg alliin). One unit of alliinase is defined as the amount of enzyme needed to produce 1 mcmol of pyruvate from alliin per minute. The amount of allicin produced was confirmed by a high-performance liquid chromatography analysis of a sample.

Allicin was prepared daily for our animal studies by reacting alliin and alliinase. Alliin was produced by a modified method developed by Stoll and Seebeck. The chemical and spectral properties of the synthetic alliin were identical to those of the natural product in the garlic clove. Alliinase extraction and purification were performed as described previously. The enzymatic activity of alliinase and the rate of production of allicin and pyruvate were determined by spectrophotometry in a coupled reaction which uses reduced nicotinamide adenine dinucleotide and lactic dehydrogenase to generate nicotinamide dinucleotide and lactic acid. The allicin was prepared just before administration by interaction of alliin (10 mg/kg rabbit) with purified alliinase (3 U/mg alliin). One unit of alliinase is defined as the amount of enzyme needed to produce 1 mcmol of pyruvate from alliin per minute. The amount of allicin produced was confirmed by a high-performance liquid chromatography analysis of a sample.

Allicin was prepared daily for our animal studies by reacting alliin and alliinase. Alliin was produced by a modified method developed by Stoll and Seebeck. The chemical and spectral properties of the synthetic alliin were identical to those of the natural product in the garlic clove. Alliinase extraction and purification were performed as described previously. The enzymatic activity of alliinase and the rate of production of allicin and pyruvate were determined by spectrophotometry in a coupled reaction which uses reduced nicotinamide adenine dinucleotide and lactic dehydrogenase to generate nicotinamide dinucleotide and lactic acid. The allicin was prepared just before administration by interaction of alliin (10 mg/kg rabbit) with purified alliinase (3 U/mg alliin). One unit of alliinase is defined as the amount of enzyme needed to produce 1 mcmol of pyruvate from alliin per minute. The amount of allicin produced was confirmed by a high-performance liquid chromatography analysis of a sample.