[Purification and characterization of two peroxidases from hard wheat].
Biochimie, 1975;57(2):145-53.
Jeanjean MF, Kobrehel K, Feillet P
PMID: 237578
Impact factor: 4.372
Abstract
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.
MeSH terms
Amino Acids; Calcium; Chemical Precipitation; Chromatography, DEAE-Cellulose; Chromatography, Gel; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Hydrogen-Ion Concentration; Kinetics; Molecular Weight; Oxidation-Reduction; Peroxidases; Spectrophotometry; Temperature; Triticum
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