Purification and characterization of paraoxonase 1 (PON1) from Swiss Black, Holstein, and Montofon bovines.

Paraoxonase 1 (PON1: EC 3.1.8.

Purification of Holstein bull semen paraoxonase 1 (PON1) by hydrophobic interaction chromatography and investigation of its inhibition kinetics by heavy metals.

In this study, paraoxonase 1 (PON1; EC 3.1.8.

Purification, characterization, and investigation of in vitro inhibition by metals of paraoxonase from different sheep breeds.

Paraoxonase (PON) was purified and characterized from the Merino and Kivircik sheep's blood serums by a two-step procedure using ammonium sulphate precipitation and Sepharose-4B-L-tyrosine-1-napthylamine hydrophobic interaction chromatography for the first time. On SDS-polyacyrilamide gel electrophoresis, purified human serum paraoxonase yielded a single band of 66 kDa on SDS-PAGE. The KM and Vmax were 0.

In vitro efficacy of some cattle drugs on bovine serum paraoxonase 1 (PON1) activity.

Serum paraoxonase 1 (EC 3.1.8.

Carbonic anhydrase inhibitors: purification and inhibition studies of pigeon (Columba livia var. domestica) red blood cell carbonic anhydrase with sulfonamides.

A carbonic anhydrase (CA, EC 4.2.1.

Carbonic anhydrase inhibitors. Inhibition of red blood cell ostrich (Struthio camelus) carbonic anhydrase with a series of aromatic and heterocyclic sulfonamides.

The purification of red blood cell carbonic anhydrase (CA, EC 4.2.1.