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The biochemistry of oligomycin resistance in mutants of the yeast Saccharomyces cerevisiae

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Broughall, John Morton (1973) The biochemistry of oligomycin resistance in mutants of the yeast Saccharomyces cerevisiae. PhD thesis, University of Warwick.

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Official URL: http://webcat.warwick.ac.uk/record=b1736248~S1

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Abstract

The biochemistry of certain oligomycin resistant mutants of the yeast Saccharomyces cerevisiae D22 has been studied. During the course of this investigation various techniques have been used and as a result of one of the methods used ideas have been proposed on the mode of oligomycin and aurovertin inhibition of mitochondrial energy linked functions.

The interaction of DCCD with yeast SMP membranes has also been studied and a mechanism for the inhibition of yeast SMP ATPase activity is proposed. This mechanism closely resembles the inhibition of red blood cell ATPase activity by carbodi-imides but it is different from the postulated mechanism of DCCD inhibition of beef heart mitochondrial ATPase activity.

Both yeast SMP membranes and a soluble oligomycin sensitive ATPase from these SMP have been used for a comparative study of the parental and oligomycin resistant strains. No gross changes were evident in the whole SMP membrane structure, but there were differences seen in the local lipid environment around the ATPase complex. These differences appeared to be related to differences in the oligomycin sensitivity of the ATPase complex. The importance of lipids within the ATPase complex is further illustrated by a new solvent extraction technique which removes oligomycin sensitivity from the SMP ATPase activity.

Item Type: Thesis or Dissertation (PhD)
Subjects: Q Science > QD Chemistry
Library of Congress Subject Headings (LCSH): Saccharomyces cerevisiae, Yeast fungi -- Biotechnology, Saccharomyces -- Biotechnology, Saccharomyces, Biochemistry
Official Date: March 1973
Dates:
DateEvent
March 1973Submitted
Institution: University of Warwick
Theses Department: Department of Chemistry
Thesis Type: PhD
Publication Status: Unpublished
Extent: 107 leaves
Language: eng

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