Home LiteratureArticle Details
PMID: 4502945 Published · ppublish English Journal Article

Genetic variants of glucose 6-phosphate dehydrogenase from human erythrocytes: unique properties of the A - variant isolated from "deficient" cells.

Babalola O, Cancedda R, Luzzatto L

Abstract

The A(-) type of glucose 6-phosphate dehydrogenase (EC 1.1.1.49) has been isolated from human erythrocytes deficient in this enzyme. The specific activity of the purified protein is similar to that previously reported for the enzyme isolated from normal, nondeficient erythrocytes. During the purification procedure, a portion of the A(-) enzyme converts spontaneously, from the native "fraction I", to a "fraction II" having different kinetic and chromatographic properties. The conversion of fraction I to II can be reproduced freely by treatment with iodosobenzoate, and fraction II can be converted back to fraction I by treatment with dithioglycol. We suggest that fraction II is an enzyme species in which one or more sulfhydryl groups have been oxidized to disulfide(s). The tendency to oxidation appears to be a property specific to the A(-) variant and may represent the basis for its rapid rate of inactivation and consequent deficiency in vivo.

MeSH Terms
Blood Protein Electrophoresis Centrifugation, Density Gradient Chromatography, Gel Disulfides/biosynthesis Electrophoresis, Starch Gel Enzyme Activation Erythrocytes/enzymology Genetic Variation Glucosephosphate Dehydrogenase/blood,isolation & purification Humans Kinetics Models, Structural Molecular Biology Oxidation-Reduction Protein Conformation Sulfhydryl Compounds/metabolism Temperature
Chemicals
Disulfides Sulfhydryl Compounds Glucosephosphate Dehydrogenase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Babalola O
Cancedda R
Luzzatto L
References (24)
24 references, click to expand
  1. Distinctive patterns of NADP binding to dimeric and tetrameric glucose 6-phosphate dehydrogenase from human red cells.
    Biochem Biophys Res Commun. 1970 Apr 8;39(1):142-8 PMID: 4392409
  2. Erythrocyte glucose-6-phosphate dehydrogenase deficiency: evidence of differences between Negroes and Caucasians with respect to this genetically determined trait.
    J Clin Invest. 1959 Dec;38:2253-62 PMID: 14421318
  3. 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):483-90 PMID: 5492291
  4. Glucose 6-phosphate dehydrogenase from human erythrocytes. II. Subactive states of the enzyme from normal persons.
    J Biol Chem. 1962 Jul;237:2371-6 PMID: 14456317
  5. Electrophoretic behaviour of human erythrocyte glucose 6-phosphate dehydrogenase during purification.
    Biochem Biophys Res Commun. 1968 May 10;31(3):501-7 PMID: 5653659
  6. 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 PMID: 5781268
  7. Negro variant of glucose-6-phosphate dehydrogenase deficiency (A-) in man.
    Science. 1967 Jan 6;155(3758):97-9 PMID: 6015571
  8. Human erythrocyte glucose 6-phosphate dehydrogenase. I. Isolation and properties of the enzyme.
    J Biol Chem. 1963 Jul;238:2309-16 PMID: 14021229
  9. In vivo lability of glucose-6-phosphate dehydrogenase in GdA- and GdMediterranean deficiency.
    J Clin Invest. 1968 Apr;47(4):940-8 PMID: 5641629
  10. Different properties of glucose 6-phosphate dehydrogenase from human erythrocytes with normal and abnormal enzyme levels.
    Biochem Biophys Res Commun. 1965 Dec 21;21(6):547-54 PMID: 4379668
  11. A single amino Acid substitution (asparagine to aspartic Acid) between normal (b+) and the common negro variant (a+) of human glucose-6-phosphate dehydrogenase.
    Proc Natl Acad Sci U S A. 1967 Mar;57(3):835-40 PMID: 16591538
  12. Enzymic properties of different types of human erythrocyte glucose-6-phosphate dehydrogenase, with characterization of two new genetic variants.
    J Clin Invest. 1968 Aug;47(8):1833-42 PMID: 5666113
  13. DIFFERENT ENZYMIC EXPRESSIONS OF MUTANTS OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE.
    Proc Natl Acad Sci U S A. 1960 Jul;46(7):938-44 PMID: 16590696
  14. Electrophoretic heterogeneity of glucose-6-phosphate dehydrogenase and its relationship to enzyme deficiency in man.
    Proc Natl Acad Sci U S A. 1962 Oct 15;48:1868-76 PMID: 14014720
  15. Glucose 6-phosphate dehydrogenase of human erythrocytes. I. Purification and characterization of normal (B+) enzyme.
    J Biol Chem. 1966 Nov 10;241(21):4966-76 PMID: 4380840
  16. Regulation of the activity of glucose-6-phosphate dehydrogenase by NADP+ and NADPH.
    Biochim Biophys Acta. 1967 Sep 12;146(1):18-25 PMID: 4383500
  17. Effects of glucose-6-phosphate dehydrogenase deficiency upon the host and upon host-drug-malaria parasite interactions.
    Mil Med. 1966 Sep;131(9):Suppl:1039-56 PMID: 4957809
  18. The role of sulfhydryl groups in the activity of D-glyceraldehyde 3-phosphate dehydrogenase.
    J Biol Chem. 1953 Sep;204(1):265-81 PMID: 13084599
  19. Isolation and purification of human erythrocyte glucose-6-phosphate dehydrogenase from small amounts of blood.
    Biochim Biophys Acta. 1969 May;181(1):1-11 PMID: 4389385
  20. Erythrocyte glucose 6-phosphate dehydrogenase of normal and mutant human subjects: properties of the purified enzymes.
    J Biol Chem. 1961 Jan;236:10-7 PMID: 13766962
  21. Purification of glucose 6-phosphate dehydrogenase from human erythrocytes.
    Ital J Biochem. 1970 May-Jun;19(3):165-77 PMID: 5500440
  22. DITHIOTHREITOL, A NEW PROTECTIVE REAGENT FOR SH GROUPS.
    Biochemistry. 1964 Apr;3:480-2 PMID: 14192894
  23. Genetic variants of human erythrocyte glucose 6-phosphate dehydrogenase. I. Regulation of activity by oxidized and reduced nicotinamide-adenine dinucleotide phosphate.
    Biochemistry. 1971 Feb 2;10(3):415-9 PMID: 5543967
  24. Resolution of genetic variants of human erythrocyte glucose 6-phosphate dehydrogenase by thin-layer chromatography.
    Biochem Biophys Res Commun. 1967 Dec 15;29(5):705-9 PMID: 6077807
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1972-04-00
Pages
946-50
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC426601
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com