The structure of rat liver mitochondria: a reevaluation |
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| Authors: | J T Brandt A P Martin F V Lucas M L Vorbeck |
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| Institution: | Department of Chemistry, Biochemistry and Biophysics Program, University of Notre Dame, Notre Dame, Indiana 46556 USA |
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| Abstract: | A β-N-acetylgalactosaminyltransferases (Ga1NAcT) that catalyzes the synthesis of a triglycosylceramide, GanglioTricer (Ga1NAcβ-Ga1β1-4G1c-cer), from lactosylceramide and UDP-Ga1NAc was isolated from guinea pig bone marrow. The enzyme was present in the supernatant solution obtained after homogenization of guinea pig bone marrow 12,000 × g pellet with 0.32 M sucrose containing 0.6% Triton X-100 and centrifugation at 129,000 × g. The enzyme that catalyzed the transfer of Ga1NAc to a tetraglycosylceramide (Lac-nTet-cer) was found in a membrane-bound fraction. The Km values were 0.5 mM and 0.7 mM for the lactosylceramide and Lac-nTet-cer, respectively. 97.0% of the terminal 14C]Ga1NAc was cleaved by the action of pure β-hexosaminidase from 14C]triglycosylceramide. |
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| Keywords: | To whom request for reprints should be sent |
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