Use this URL to cite or link to this record in EThOS: https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.796372
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.
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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