[Purification and characterization of two peroxidases from hard wheat].
Two peroxidases A and B were purified from a borate buffer extract (pH = 10,4) of durum wheat semolina (Triticum durum), var. Bidi 17, by chromatography on DEAE-cellulose, salting out by 3M ammonium sulphate and two chromatographies on CM-cellulose; specific activities of peroxidase A or B were increased 114 or 66 fold. Molecular weight, amino acid composition, absorption spectrum, pH optimum, thermal stability and KM values differentiate the two enzymes. Ion Ca++ was shown as an activator of both peroxidase activities; the presence of an inhibitor in the crude extract was demonstrated.
D000596:Amino Acids / Q000032:analysis; D002118:Calcium / Q000494:pharmacology; D011232:Chemical Precipitation; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000032:analysis / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D013053:Spectrophotometry; D013696:Temperature; D014908:Triticum / Q000201:enzymology*
D000596:Amino Acids; D010544:Peroxidases; D002118:Calcium
Purification et caractérisation de deux peroxydases de blé dur