Purification and Characterization of Peroxidase from Sweet Gourd (Cucurbita moschataLam. Poiret)

Abstract

Peroxidase (EC 1.11.1.7; donor: hydrogen peroxide oxidoreductase) is an oxidoreductase enzyme found in many fruits and vegetables. This enzyme was purified from sweet gourd (Cucurbita moschata Lam. Poiret) by ammonium sulphate precipitation and CM-Sephadex ion-exchange chromatography. Furthermore, optimum pH, optimum temperature, optimum ionic strength, stable pH, and stable temperature conditions were determined as 7.2, 50 • C, 0.4 M, 8.0, and 40 • C, respectively. The molecular weight (M W ) of the enzyme was estimated to be 85 kDa by SDS-PAGE method. The values of K m and V max were calculated from the Lineweaver-Burk graph for guaiacol/H 2 O 2 substrate patterns.

The effects of some bromophenols on human carbonic anhydrase isoenzymes

“…They were frequently isolated from red algae of the family Rhodomelaceae and had some important biological activities [53][54][55] . It was reported that the bromophenol derivatives coordinate to the active site Zn 2+ and to block the reaction catalysis.…”

Synthesis of N-alkyl (aril)-tetra pyrimidine thiones and investigation of their human carbonic anhydrase I and II inhibitory effects

“…Then, the purification process was realised. The protein flow in the column effluents was determined spectrophotometrically at 280 nm as previously reported [64][65][66] . Both isoenzymes purities were controlled by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) according to Laemmli's method 67 .…”

Synthesis and inhibitory properties of some carbamates on carbonic anhydrase and acetylcholine esterase

“…Then, supernatant was transferred to the previously prepared Sepharose-4B-L-tyrosine-sulphanilamide affinity column 50 . Subsequently, the proteins from the column were spectrophotometrically determined at 280 nm [79][80][81][82][83][84][85] . For determination of the purity of the hCA isoenzymes, sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), having 10 and 3% acrylamide as an eluent and packing gel, respectively, with 0.1% SDS [86][87][88][89][90] , was performed, through which a single band was observed for each isoenzyme.…”