Use this URL to cite or link to this record in EThOS: | https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.796372 |
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Title: | Structural and functional studies on component X of mammalian pyruvate dehydrogenase multienzyme complex | ||||||
Author: | Neagle, James Campbell | ||||||
Awarding Body: | University of Glasgow | ||||||
Current Institution: | University of Glasgow | ||||||
Date of Award: | 1990 | ||||||
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Abstract: | |||||||
Pyruvate dehydrogenase is a multienzyme complex consisting of three enzymes, a decarboxylase (E1l), an acetyltransferase (E2) and a dehydrogenase (E3). A fourth enzyme of unknown function component X or protein X has recently been identified. Several similarities between E2 and protein X have been demonstrated. Further investigation into this unique polypeptide has shown monospecificity of antiserum raised against gel purified protein X and E2. In various cell lines, antiserum to protein X failed to recognise the E2 component, similarly with E2 antiserum no cross reactivity with protein X polypeptide was observed.
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Supervisor: | Not available | Sponsor: | Not available | ||||
Qualification Name: | Thesis (Ph.D.) | Qualification Level: | Doctoral | ||||
EThOS ID: | uk.bl.ethos.796372 | DOI: | Not available | ||||
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