Record Details

Purification and characterization of sulfite oxidase from goat liver

NOPR - NISCAIR Online Periodicals Repository

View Archive Info
 
 
Field Value
 
Title Purification and characterization of sulfite oxidase from goat liver
 
Creator Ahmad, Ausaf
Ahmad, Sarfraz
Baig, Masroor A
 
Subject Goat liver
Sulfite oxidase
Molybdoenzyme
Molybdenum
Heme
Purification
Physico-chemical properties
CD spectra
Absorption spectra
N-terminal analysis
 
Description 379-386
Sulfite oxidase (EC 1.8.3.1) catalyzes the physiologically vital oxidation of sulfite to sulfate, the terminal reaction in the degradation of sulfur containing amino acids. Genetic deficiency related to human sulfite oxidase is associated with the severe clinical abnormalities with no effective therapies known, making the enzyme of immense biomedical importance. In the present study, sulfite oxidase was been purified from the goat tissues, a hitherto unexplored source, in particular from the liver, and its physico and biochemical properties were characterized. The liver was chosen as it showed the highest activity, compared to kidney and muscle. The enzyme was purified to homogeneity by salting out, gel filtration and ion-exchange chromatography. It was a dimer (113 kDa) having two identical subunits (56 kDa) and did not contain free sulfhydryl groups. Its spectral analysis showed the presence of heme and molybdenum. circular dichroism (CD) spectra in near and far-UV regions showed the presence of significant amounts of secondary structures (45% ⍺ helix, 9% β structure and 26% β turn and remaining random coil) in the native molecule. The kinetic and hydrodynamic properties of the enzyme were also determined. Results also showed that ferricyanide was 8-times more effective electron acceptor than its physiological acceptor cytochrome c. The limited N-terminal analysis of the enzyme revealed the sequence up to six amino acids Trp-Glu-Pro-Ser-Gly-Ala. Together, these results suggested the liver was a major source of sulfite oxidase in goat and most of its physico-chemical, except secondary structure and amino acid sequence from N-terminal and biological properties were fairly similar to the sulfite oxidase isolated from other mammalian species/organs.
 
Date 2008-12-31T05:52:01Z
2008-12-31T05:52:01Z
2008-12
 
Type Article
 
Identifier 0301-1208
http://hdl.handle.net/123456789/2704
 
Language en_US
 
Publisher CSIR
 
Source IJBB Vol.45(6) [December 2008]