(Z)-3-(4-bromophenyl)-3-(3-pyridyl)allylamine as substrate for studies of myeloperoxidase activity.

(Z)-3-(4-Bromophenyl)-3-(3-pyridyl)allylamine (CPP 200) is transformed to the corresponding chloroimine by hypochlorite ion (ClO-) formed in the presence of myeloperoxidase. A scheme for this transformation is given. The influence of various compounds on this process has been studied. Cysteamine, cysteine and 6-chloro-3-hydrazino-pyridazine inhibited the transformation of CPP 200, while some p-hydroxyphenyl derivatives increased the rate of transformation of CPP 200. The increase seen on addition of the p-hydroxyphenyl derivatives is not a chloride-dependent reaction. Various mechanisms for the inhibiting effect as well as for the activating effect on the transformation of CPP 200 are discussed.