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dc.contributor.authorRyan, Eric D.
dc.contributor.authorTracy, James W.
dc.contributor.authorKohlhaw, Gunter B.
dc.identifier.citationRyan, E. D., Tracy, J. W., & Kohlhaw, G. B. (1973). Subcellular Localization of the Leucine Biosynthetic Enzymes in Yeast. Journal of Bacteriology, 116(1), 222–225.en_US
dc.description.abstractWhen baker's yeast spheroplasts were lysed by mild osmotic shock, practically all of the isopropylmalate isomerase and the β-isopropylmalate dehydrogenase was released into the 30,000 × g supernatant fraction, as was the cytosol marker enzyme, glucose-6-phosphate dehydrogenase. α-Isopropylmalate synthase, however, was not detected in the initial supernatant, but could be progressively solubilized by homogenization, appearing more slowly than citrate synthase but faster than cytochrome oxidase. Of the total glutamate-α-ketoisocaproate transaminase activity, approximately 20% was in the initial soluble fraction, whereas solubilization of the remainder again required homogenization of the spheroplast lysate. Results from sucrose density gradient centrifugation of a cell-free particulate fraction and comparison with marker enzymes suggested that α-isopropylmalate synthase was located in the mitochondria. It thus appears that, in yeast, the first specific enzyme in the leucine biosynthetic pathway (α-isopropylmalate synthase) is particulate, whereas the next two enzymes in the pathway (isopropylmalate isomerase and β-isopropylmalate dehydrogenase) are “soluble,” with glutamate-α-ketoisocaproate transaminase activity being located in both the cytosol and particulate cell fractions.en_US
dc.publisherAmerican Society for Microbiologyen_US
dc.titleSubcellular Localization of the Leucine Biosynthetic Enzymes in Yeasten_US
kusw.kuauthorTracy, James
kusw.kudepartmentPharmacology & Toxicologyen_US
kusw.oanotesPer SHERPA/RoMEO 7/22/2016: Author's Pre-print: green tick author can archive pre-print (ie pre-refereeing) Author's Post-print: green tick author can archive post-print (ie final draft post-refereeing) Publisher's Version/PDF: green tick author can archive publisher's version/PDF General Conditions:

Author's pre-print on recognised non profit pre-print archives Author's post-print on funder's repositories, institutional repository or subject-based repositories Non-commercial Publisher's version/PDF may be used Publisher's version/PDF may be used on author's personal website or employers website Recommended that author's post-prints submitted to PubMed or institutional repositories are made available 6 months after publication Author's pre-print must be updated with citation and DOI upon publication
kusw.oaversionScholarly/refereed, publisher versionen_US
kusw.oapolicyThis item does not meet KU Open Access policy criteria.en_US

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