Fortgesetzte Versuche über synthetische Häminkatalasen. 7. Mitteilung über Katalase.

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Abstract
The catalase activity, pH optimum, and absorption spectrum of complexes of parahaematin and haemochromogen with various amino acids, organic bases, and native and denatured proteins were studied. The protein complexes showed a lower activity than the uncombined hematin or hemochromogen. The amino acids and piperazine and quinoline were without effect. Coupling with isatin increased the activity somewhat. All of these measured activities were only about a 10-6 fraction of that of natural catalase. Adsorption of such complexes on charcoal changed the pH optimum and produced good oxygen carriers but caused little change in catalase activity. Absorption spectrum and pH optimum observations pointed to the parahaematin compounds as most closely related to natural catalase.

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