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Original Articles

Variazioni di attività della clorogenico ossidasi e di altri enzimi interessati all'ossidoriduzione del TPN durante l'attivazione di fettine di tubero di patata

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Pages 250-266 | Received 17 Dec 1961, Published online: 14 Sep 2009
 

Abstract

CHANGES IN THE ACTIVITY OF CHLOROGENIC ACID OXIDASE AND OTHER ENZYMES INVOLVED IN OXIDATION AND REDUCTION OF TPN IN AGEING POTATO TUBER SLICES. — The activation of respiration, and in particular of the pentose phosphate pathway, during incubation of potato tuber slices could depend on the increase of activity of oxidative enzymes mediating electron transfer from Gl. 6-P to oxygen.

The present report deals with the activity changes, in the first period of incubation, of the following enzymes: Gl. 6-P-dehydrogenase, TPNH-glutathione reductase, gluta-thione-dehydroascorbate reductase, chlorogenic acid oxidase and a TPNH diaphorase utilizing tetrazolium salts as electron acceptors.

The activity of all of these enzymes, with the exception of TPNH diaphorase, was found to bs, at all stages of incubation, in large excess respect that required to account for the estimated contribution of the pentose phosphate pathway to respiration.

Gl. 6-P dehydrogenase, glutathione reductase and chlorogenic oxidase activities markedly incresed during incubation; but their increase appeared to be clearly delayed (of some hours) respect that of oxygen uptake. This seems to indicate that the increase in activity of these anzymes is rather a consequence than a cause of the respiratory activation.

TPNH diaphorase showed a very low activity in the fresh slices, and it increased quite significantly already in the very first period (5 hours) of incubation. This behaviour suggests the possibility that this enzyme could limit TPNH oxidation, and thus the pentose phosphate pathway activity, and that its activation could be correlated with that of oxidative metabolism in the ageing slices. Further investigation of this hypothesis requires the identification of the natural electron acceptor of this enzyme.

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