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C Bernofsky

Publications and source records attributed to C Bernofsky.

9 recordsLinked to original sources

Mitochondrial glucose-6-phosphate dehydrogenase from Saccharomyces cerevisiae.

In Saccharomyces cerevisiae, a small proportion of the glucose-6-P dehydrogenase activity is firmly associated with the mitochondrial fraction and is not removed by repeated washing or density-gradient centrifugation. However, the enzyme is released by sonic disruption. Mitochondrial glucose-6-P dehydrogenase that is released by sonication and partially purified has been found to be similar to cytosol glucose-6-P dehydrogenase with respect to electrophoretic mobility, isoelectric point, pH optimum, molecular size, and apparent KM's for NADP+ and glucose-6-P. These results indicate that a single species of glucose-6-P dehydrogenase is synthesized in S. cerevisiae and that the enzyme has more than one intracellular location. Mitochondrial glucose-6-P dehydrogenase may be a source of intramitochondrial NADPH and may function with hexokinase and transhydrogenase to provide a pathway for glucose oxidation that is coupled to the synthesis of mitochondrial ATP. A constant proportion of total glucose-6-P dehydrogenase activity remains compartmented in the mitochondrial fraction throughout the growth cycle.

Cell Cycle

Evidence for the multiplicity of products from acid-treated reduced nicotinamide adenine dinucleotide (NADH).

Treatment of NADH with acid gives rise to as many as 10 products derived from breakdown of the dihydropyridine ring. These substances are neutral or cationic in character, and one or more may be carbonyls. They have been separated on a column of Dowex 1-formate and characterized spectrophotometrically. No evidence was obtained to indicate that acidification of NADH leads to formation of a dinucleotide containing a modified dihydronicotinamide moiety.

Cell Line