Untersuchungen an künstlichen Peroxydasen.

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Abstract
Peroxidase (I) of horseradish was split into hemin and free protein (II) by means of HCl -acetone. II was coupled with synthetic hemins (III) to produce active and inactive "synthetic peroxidases." The coupling reaction, which was probably of the first order, was followed spectrophotometrically. Their activities with various III were: proto-I, 100%; deutero-I, 56%; meso-I, 63%; aza-I, 20%; phaophorbid a-I, 0% and chlorin c6-I, 0%. Free protein reacting with phaeophorbid a-hemin did not interfere with coupling of protohemin. Both I of horseradish and its protein component were stable when heated to 62[degree] and 69[degree] resp. for 15 minutes. Very pure distilled water, having a minimum amt. of metal impurities was required for the exptl. procedure.

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