Purification and yield of a cationic peroxidase from a peanut suspension cell culture

Variability in the purity of peanut ( Arachis hypogaea ) peroxidase has necessitated the introduction of further purification steps beyond those used formerly. This appeared to be necessary when the purity of the peroxidase obtained by the established approach was found to be deficient as determined by electrophoresis and by absorption spectra. The addition of lectin affinity and gel filtration steps yielded a homogeneous preparation as indicated by polyacrylamide gel electrophoresis (PAGE) of 20 μg of protein on a mini gel. The RZ (405/280 nm) value was as good as the best former values. A calculation of the capacity of the cultured peanut cells to produce the highly purified peroxidase is presented.