Purification of xanthine oxidase from bovine milk by affinity chromatography with a novel gel.

A new affinity gel was synthesized for the purification of xanthine oxidase (XO, EC 1.2.3.

Synthesis of a novel affinity gel for the purification of carbonic anhydrases.

A new affinity gel was synthesized for the purification of carbonic anhydrase (CA, EC 4.2.1.

Carbonic anhydrase inhibitors. Phenols incorporating 2- or 3-pyridyl-ethenylcarbonyl and tertiary amine moieties strongly inhibit Saccharomyces cerevisiae β-carbonic anhydrase.

A series of phenols incorporating tertiary amine and trans-pyridylethenyl-carbonyl moieties were assayed as inhibitors of the β-carbonic anhydrase (CA, EC 4.2.1.

In vitro effect of novel β-lactam compounds on xanthine oxidase enzyme activity.

Carbazole substituted imines (2a-l) were prepared from N-methyl-3-amino carbazole with different aldehydes. The imines compounds undergo (2+2) cycloaddition reactions with in situ ketenes to produce β-lactam compounds (3a-l). The β-lactam compounds were tested as inhibitors of the xanthine oxidase (XO) purified from bovine milk.

Investigation of heavy metal effects on immobilized paraoxanase by glutaraldehyde.

Serum paraoxonase 1 (PON1) was purified from bovine serum using hydrophobic interaction chromotography on Sepharose 4B-coupled l-tyrosine 1-naphthylamine gel, and monitored by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Paraoxonase enzyme was immobilized using different ratios of glutaraldehyde and the maximum activity was observed with 7% glutaraldehyde. The effects of inhibition by Mn(+2), Co(+2) and Cu(+2) heavy metals on the immobilized and free enzyme activities were studied.