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The Chemistry of Experimental Chloroma

III. Activity and Activation of VPO in Cellular Particulates^*

( Samuel S. Fels Research Institute, Temple University School of Medicine, Philadelphia, Pa.)

A supernatant which showed that the activation of VPO activity was free of mitochondria (to succinoxidase activity) contained a hemeprotein whose reduced-difference spectrum had a peak at 430 and a CO-reduced peak at 420, fluoresced yellow under ultraviolet light, and was not sedimented at 25,000 g after 1 hour. The fact that hemoglobin did not affect the activity of VPO does not eliminate the 430 peak as being due to hemoglobin. However, the 430 compound was associated with factors containing the activator. Part of the unusually high peroxidase activity may be accounted for by the presence of this activator rather than by the verdoperoxidase per se. If due to the former, one would expect to isolate a great deal less than would be expected from the activity.

^* This investigation was supported by a research grant C-1966 (C2) from the National Cancer Institute of the National Institutes of Health, Public Health Service.

Received 12/19/55.