Purification and Properties of NADP+-linked Glycerol Dehydrogenase from Neurospora crassa

References

1. Ben-Amotz A., Avron M. 1973; NADP specific dihydroxyacetone reductase from Dunaliella parva. FEBS Letters 29:153–155
   [Google Scholar]
2. Ben-Amotz A., Avron M. 1974; Isolation, characterization, and partial purification of a reduced nicotinamide adenine dinucleotide phosphate-dependent dihydroxyacetone reductase from the halophilic alga Dunaliella parva. Plant Physiology 53:628–631
   [Google Scholar]
3. Bergmeyer H. U. 1974; Procedures related to enzymatic analysis. In Methods of Enzymatic Analysis171–176 Bergmeyer H. U. New York: Academic Press;
   [Google Scholar]
4. Böhme H.-J., Kopperschlager G., Schulz J., Hofmann E. 1972; Affinity chromatography of phosphofructokinase using Cibacron blue F3G-A. Journal of Chromatography 69:209–214
   [Google Scholar]
5. Bosron W. F., Prairie R. L. 1972; Triphospho-pyridine nucleotide-linked aldehyde reductase. I. Purification and properties of the enzyme from pig kidney cortex. Journal of Biological Chemistry 247:4480–4485
   [Google Scholar]
6. Davis B. J. 1964; Disc electrophoresis. II. Method and applications to human serum proteins. Annals of the New York Academy of Sciences 121:404–427
   [Google Scholar]
7. Dutler H., Van der Baan J. L., Hochuli E., Kis Z., Taylor K. E., Prelog V. 1977; Dihydroxyacetone reductase from Mucor javanicus. I. Isolation and properties. European Journal of Biochemistry 75:423–432
   [Google Scholar]
8. Fairbanks G., Steck T. L., Wallach D. F. H. 1971; Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10:2606–2617
   [Google Scholar]
9. Good N. E., Winget G. D., Winter W., Con-nally T. N., Izawa S., Singh R. M. M. 1966; Hydrogen ion buffers for biological research. Biochemistry 5:467–477
   [Google Scholar]
10. Hochuli E., Taylor K. E., Dutler H. 1977; Dihydroxyacetone reductase from Mucor javanicus. 2. Identification of the physiological substrate and reactivity towards related compounds. European Journal of Biochemistry 75:433–439
    [Google Scholar]
11. Keilin D., Hartree E. F. 1938; On the mechanism of the decomposition of hydrogen peroxide by catalase. Proceedings of the Royal Society B124397–405
    [Google Scholar]
12. Kormann A. W., Hurst R. O., Flynn T. G. 1972; Purification and properties of an NADP⁺-dependent glycerol dehydrogenase from rabbit skeletal muscle. Biochimica et biophysica acta 258:40–55
    [Google Scholar]
13. Lin E. C. C. 1976; Glycerol dissimilation and its regulation in bacteria. Annual Review of Micro-biology 30:535–578
    [Google Scholar]
14. Otavsky W. I., Drysdale J. W. 1975; Recent staining artifacts with LKB ‘ampholines’ on gel isoelectric-focusing. Analytical Biochemistry 65:533–536
    [Google Scholar]
15. Sheys G. H., Arnold W. J., Watson J. A., Hayashi J. A., Doughty C. C. 1971; Aldose reductase from Rhodotcrula. I. Purification and properties. Journal of Biological Chemistry 246:3824–3827
    [Google Scholar]
16. Sheys G. H., Doughty C. C. 1971a; Subunits of aldose reductase from Rhodotorula. Biochimica et biophysica acta 235:414–417
    [Google Scholar]
17. Sheys G. H., Doughty C. C. 1971b; The reaction mechanism of aldose reductase from Rhodotorula. Biochimica et biophysica acta 242:523–531
    [Google Scholar]
18. Toews C. J. 1966; Evidence for the metabolism of glycerol by skeletal muscle and presence of a muscle nicotinamide-adenine dinucleotide phosphate-dependent glycerol dehydrogenase. Biochemical Journal 98:27c–29c
    [Google Scholar]
19. Toews C. J. 1967; The kinetics and reaction mechanism of the nicotinamide-adenine dinucleotide phosphate-specific glycerol dehydrogenase of rat skeletal muscle. Biochemical Journal 105:1067–1073
    [Google Scholar]
20. Viswanath-Reddy M., Bennett S. N., Howe H. B. 1977; Characterization of glycerol non-utilizing and protoperithecial mutants of Neurospora. Molecular and General Genetics 153:29–38
    [Google Scholar]
21. Westergaard M., Mitchell H. K. 1947; Neurospora. V. A synthetic medium favouring sexual reproduction. American Journal of Botany 34:573–577
    [Google Scholar]