Abstract
The enzymic coupling of catharanthine and vindoline can be performed with plant peroxidases
in a reaction which yields 3′,4′-anhydrovinblastine (AVLB) as the major product. This
has led to an investigation of other sources of peroxidase activity and haem. High
levels of AVLB were obtained using microperoxidase (haem-undecapeptide) and haemin,
and lower yields were also detected with lactoperoxidase, cytochrome C, and haemoglobin.
The activity with haemin and microperoxidase has been optimized and it is concluded
that, in comparison with horseradish peroxidase, these systems provide an improved
means of coupling.
