Products of alkaloid oxidation by blood plasma hemoprotein

Elaev, N. R.; Ryzhakov, A. V.

doi:10.1007/bf00839995

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1988

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“…The mechanism of coupling with microperoxidase and haemin in the absence of H202 is not immediately obvious, but it does indicate that an alternative coupling mechanism can occur. A blood haemoprotein has been shown to oxidize the alkaloids arecoline and atropine to their N-oxides in the absence of H202 (18) and perhaps a similar phenomenon occurs with catharanthine in the presence of these haems. In the modified Polonovski coupling method, eatharanthine is converted to its N-oxide prior to incubation with vindoline.…”

Section: Resultsmentioning

confidence: 97%

The Coupling of Catharanthine and Vindoline to Form 3′,4′-Anhydrovinblastine by Haemoproteins and Haemin

Goodbody

Endo²,

Vukovic³

et al. 1988

Planta Med

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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.

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Section: Resultsmentioning

confidence: 97%