Abstract
Glucose-6-phosphate dehydrogenase has been purified to near homogeneity from wild-type Escherichia coli K-12 and from a mutant previously found to contain substantially more of the enzyme. The two enzymes are the same in all characteristics studied thus far: specific activity, kinetics, specificity, and subunit size.
Full text
PDF





Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bonsignore A., Lorenzoni I., Cancedda R., Cosulich M. E., De Flora A. Effect of divalent cations on the structure of human erythrocyte glucose 6-P dehydrogenase. Biochem Biophys Res Commun. 1971 Jan 22;42(2):159–165. doi: 10.1016/0006-291x(71)90082-9. [DOI] [PubMed] [Google Scholar]
- Cohen P., Rosemeyer M. A. Human glucose-6-phosphate dehydrogenase: purification of the erythrocyte enzyme and the influence of ions on its activity. Eur J Biochem. 1969 Mar;8(1):1–7. doi: 10.1111/j.1432-1033.1969.tb00487.x. [DOI] [PubMed] [Google Scholar]
- DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
- Engel H. J., Domschke W., Alberti M., Domagk G. F. Protein structure and enzymatic activity. II. Purification and properties of a crystalline glucose-6-phosphate dehydrogenase from Candida utilis. Biochim Biophys Acta. 1969;191(3):509–516. doi: 10.1016/0005-2744(69)90344-1. [DOI] [PubMed] [Google Scholar]
- Fraenkel D. G., Banerjee S. A mutation increasing the amount of a constitutive enzyme in Escherichia coli, glucose 6-phosphate dehydrogenase. J Mol Biol. 1971 Feb 28;56(1):183–194. doi: 10.1016/0022-2836(71)90093-3. [DOI] [PubMed] [Google Scholar]
- JULIAN G. R., WOLFE R. G., REITHEL F. J. The enzymes of mammary gland. II. The preparation of glucose 6-phosphate dehydrogenase. J Biol Chem. 1961 Mar;236:754–758. [PubMed] [Google Scholar]
- KIRKMAN H. N., HENDRICKSON E. M. Glucose 6-phosphate dehydrogenase from human erythrocytes. II. Subactive states of the enzyme from normal persons. J Biol Chem. 1962 Jul;237:2371–2376. [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- NOLTMANN E. A., GUBLER C. J., KUBY S. A. Glucose 6-phosphate dehydrogenase (Zwischenferment). I. Isolation of the crystalline enzyme from yeast. J Biol Chem. 1961 May;236:1225–1230. [PubMed] [Google Scholar]
- Oliv C., Levy H. R. Glucose 6-phosphatedehydrogenase from Leuconostoc mesenteroides. Physical studies. J Biol Chem. 1971 Apr 10;246(7):2043–2046. [PubMed] [Google Scholar]
- Olive C., Levy H. R. The preparation and some properties of crystalline glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides. Biochemistry. 1967 Mar;6(3):730–736. doi: 10.1021/bi00855a012. [DOI] [PubMed] [Google Scholar]
- Pardee A. B., Benz E. J., Jr, St Peter D. A., Krieger J. N., Meuth M., Trieshmann H. W., Jr Hyperproduction and purification of nicotinamide deamidase, a microconstitutive enzyme of Escherichia coli. J Biol Chem. 1971 Nov 25;246(22):6792–6796. [PubMed] [Google Scholar]
- Rattazzi M. C. Glucose 6-phosphate dehydrogenase from human erythrocytes: molecular weight determination by gel filtration. Biochem Biophys Res Commun. 1968 Apr 5;31(1):16–24. doi: 10.1016/0006-291x(68)90024-7. [DOI] [PubMed] [Google Scholar]
- SCOTT D. B., COHEN S. S. The oxidative pathway of carbohydrate metabolism in Escherichia coli. 1. The isolation and properties of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Biochem J. 1953 Aug;55(1):23–33. doi: 10.1042/bj0550023. [DOI] [PMC free article] [PubMed] [Google Scholar]
- SISTROM W. R. On the physical state of the intracellularly accumulates substrates of beta-galactoside-permease in Escherichia coli. Biochim Biophys Acta. 1958 Sep;29(3):579–587. doi: 10.1016/0006-3002(58)90015-5. [DOI] [PubMed] [Google Scholar]
- Sanwal B. D. Regulatory mechanisms involving nicotinamide adenine nucleotides as allosteric effectors. 3. Control of glucose 6-phosphate dehydrogenase. J Biol Chem. 1970 Apr 10;245(7):1626–1631. [PubMed] [Google Scholar]
- Sirotnak F. M. High dihydrofolate reductase levels in Diplococcus pneumoniae after mutation in the structural gene: biochemical and immunological evidence for increased synthesis. J Bacteriol. 1971 May;106(2):318–324. doi: 10.1128/jb.106.2.318-324.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
- Yoshida A. Amino acid substitution (histidine to tyrosine) in a glucose-6-phosphate dehydrogenase variant (G6PD Hektoen) associated with over-production. J Mol Biol. 1970 Sep 28;52(3):483–490. doi: 10.1016/0022-2836(70)90414-6. [DOI] [PubMed] [Google Scholar]
- Yoshida A. Glucose 6-phosphate dehydrogenase of human erythrocytes. I. Purification and characterization of normal (B+) enzyme. J Biol Chem. 1966 Nov 10;241(21):4966–4976. [PubMed] [Google Scholar]
- Yue R. H., Noltmann E. A., Kuby S. A. Glucose 6-phosphate dehydrogenase (Zwischenferment). II. Homogeneity measurements and physical properties of the crystalline apoenzyme from yeast. Biochemistry. 1967 Apr;6(4):1174–1183. doi: 10.1021/bi00856a030. [DOI] [PubMed] [Google Scholar]