[Peroxidases of high molecular weight identified as the membrane peroxidases in lentils].

Peroxidases extracted from lentil roots are separated in two peaks by gel chromatography on Sephadex G-100 or on Bio Gel A-5 M. On both resins, the first peak of extremely large molecular weight is demonstrated to be an association of some peroxidases with microsomes. These enzymes can be detached from membranes by NaCl.

Ribosomal and mitochondrial peroxidase isoenzymes of the lentil (Lens culinaris) root.

Ribosome- and mitochondria-rich preparations were obtained from lentil roots and their peroxidase isoenzymes examined by starch gel electrophoresis. Seven isoenzymes were shown to be associated with both the ribosomal and mitochondrial fractions.The apparent similarity between ribosomal and mitochondrial isoenzyme patterns, together with the observation that a considerable amount of peroxidase activity dissociated from the ribosomes during sedimentation of the ribosomal preparation into a sucrose gradient, suggested that at least some of these isoperoxidases were attached to membranes.