two peroxidases (ec. 1.11.1.7), pod i and pod ii were purified from the roots of cultivatedraphanus sativus l. var. cicil by one step ion-exchange chromatography after fractionation by acetone. the molecular weight of these enzymes were 43000 and 41000 daltons and rz 1.2 and 2.0 for pod i and pod ii, respectively. both enzymes consisted of a single polypeptide chain on sds-page. the maximum act...

We have assigned the biosynthetic processing steps of cathepsin D to intracellular compartments which are involved in its transport to lysosomes in HepG2 cells. Cathepsin D was synthesized as a 51-kDa proenzyme. After formation of 51-55-kDa intermediates due to processing of N-linked oligosaccharides, procathepsin D was proteolytically processed to an intermediate 44-kDa and the mature 31-kDa e...

The atypical two-electron oxidation of thioanisole and its p-methyl, p-methoxy, and p-nitro analogues by horseradish peroxidase, contrary to earlier reports, stereoselectively produces the (8) sulfoxides in 6070% enantiomeric excess. Horseradish peroxidase reconstituted with 6-meso-ethylheme has little peroxidase (guaiacol oxidizing) activity, as previously reported, but exhibits increased sulf...

Horseradish peroxidase and chlorite, NaC102, are able to catalyze chlorination of monochlorodimedone to form dichlorodimedone. Catalytic amounts of horseradish peroxidase act to disproportionate chlorite forming chlorine dioxide and chloride ion. The chlorine dioxide thus formed is responsible for the chlorination of monochlorodimedone. It was previously thought (Chiang, R., Rand-Meir, T., Maki...

Hydrogen peroxide is a very reactive byproduct of many metabolic pathways. We describe an ultra-sensitive colorimetric method to detect hydrogen peroxide based on the reconstitution of apo-horseradish peroxidase with the hemin derivative, hemin di(N,N'-acetyl-hydrazide). Oxidation of the latter by hydrogen peroxide yields hemin, which is able to reconstitute apo-horseradish peroxidase, forming ...