Use this URL to cite or link to this record in EThOS: https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.795871
Title: An investigation of galacturonyltransferase activity involved in pectin biosynthesis
Author: Cumming, Carol
Awarding Body: University of Glasgow
Current Institution: University of Glasgow
Date of Award: 1987
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Abstract:
A particulate enzyme preparation, obtained from epicotyls of etiolated pea (Pisum sativum) seedlings, exhibited galacturonyltransferase activity. The enzyme preparation had the ability to incorporate galacturonic acid from UDP-galacturonic acid into pectin. The product is thought to be either homogalacturonan or rhamnogalacturonan I or both. The optimum conditions required by the particulate enzyme preparation were investigated, Galacturonyltransferase activity was shown to be higher in the region of elongation of the epicotyl but the whole epicotyl did contain galacturonyltransferase activity. Solubilisation of galacturonyltransferase activity was attempted. Partial solubilisation was achieved using the detergent LDAO but further work is required to confirm this. The effect of the presence of UDP-rhamnose and GDP-rhamnose on galacturonyltransferase activity was also investigated but no evidence was found to indicate co-operation between galacturonyltransferase and rhamnosyl transferase.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.795871  DOI: Not available
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