Home LiteratureArticle Details
PMID: 4658994 Published · ppublish English Journal Article

Studies of the denaturation and partial renaturation of ovalbumin.

The Biochemical journal ·Vol. 129 ·No. 3 ·1972-09-00 ·Pages 665-76

Holt JC, Creeth JM

Abstract

1. The denaturation of ovalbumin by the reagents sodium dodecyl sulphate and guanidinium chloride was investigated, by following the changes in sedimentation velocity, optical rotatory dispersion and viscosity as a function of denaturant concentration. 2. With sodium dodecyl sulphate both the optical-rotatory-dispersion parameters a(0) and b(0) become more negative, the sedimentation coefficient decreases and the viscosity increases; significant differences in the denaturation profiles are observed. The change in each parameter is indicative of only limited denaturation. 3. With guanidinium chloride the transition occurs over the concentration range 1-4m: more extensive changes occur in all the physical parameters than with sodium dodecyl sulphate. The values of a(0) and b(0) are indicative of complete denaturation. Reduction by mercaptoethanol produces only minor further changes. 4. Renaturation was attempted from both denaturants, the removal of reagent being accomplished reversibly by controlled slow dialysis. Partial renaturation was observed, but aggregated or insoluble material was produced in both cases at relatively low concentrations of denaturant. Similar behaviour was observed with fully reduced protein in guanidinium chloride-mercaptoethanol; complete renaturation could not be brought about even at very low protein concentrations.

MeSH Terms
Dialysis Guanidines Mercaptoethanol Optical Rotatory Dispersion Ovalbumin Oxidation-Reduction Protein Denaturation Sodium Dodecyl Sulfate Ultracentrifugation Viscosity
Chemicals
Guanidines Sodium Dodecyl Sulfate Mercaptoethanol Ovalbumin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Holt J C
Creeth J M
References (45)
45 references, click to expand
  1. A model for the myosin molecule.
    Biochim Biophys Acta. 1960 Jul 15;41:401-21 PMID: 14408979
  2. Proteins as random coils. 3. Optical rotatory dispersion in 6 M guanidine hydrochloride.
    J Am Chem Soc. 1967 Sep 13;89(19):5023-9 PMID: 6074805
  3. Kineticsspects of conformational changes in proteins. II. Structural changes in renaturation of denatured proteins.
    Biochemistry. 1971 Mar 2;10(5):798-805 PMID: 5102320
  4. Sedimentation studies with the Spinco ultracentrifuge.
    Arch Biochem Biophys. 1952 Apr;36(2):249-58 PMID: 14944249
  5. The partial specific volume of bovine plasma albumin in the presence of potassium chloride.
    J Phys Chem. 1967 Nov;71(12):3717-9 PMID: 6074041
  6. Interpretation of equilibrium sedimentation measurements of proteins in guanidine hydrochloride solutions. Partial volumes, density increments, and the molecular weight of the subunits of rabbit muscle aldolase.
    Biochemistry. 1969 Nov;8(11):4572-8 PMID: 5389439
  7. The macromolecular properties of blood-group substances. Sedimentation-velocity and viscosity measurements.
    Biochem J. 1967 Dec;105(3):1135-45 PMID: 16742540
  8. Protein denaturation. C. Theoretical models for the mechanism of denaturation.
    Adv Protein Chem. 1970;24:1-95 PMID: 4912353
  9. The binding of sodium dodecyl sulphate to various proteins.
    Biochem J. 1968 Oct;109(5):825-30 PMID: 4177067
  10. The gross conformation of protein-sodium dodecyl sulfate complexes.
    J Biol Chem. 1970 Oct 10;245(19):5161-5 PMID: 5528242
  11. Reversible denaturation of enzymes by sodium dodecyl sulfate.
    J Biol Chem. 1971 Jul 25;246(14):4504-9 PMID: 5106387
  12. Optical rotatory dispersion studies of globular proteins, including alpha-chymotrypsin. I. Effect of concentration.
    J Biol Chem. 1968 Sep 10;243(17):4615-25 PMID: 4879169
  13. Studies on the denaturation of biological macromolecules by chemical carcinogens. 3. Optical rotatory dispersion and light-scattering changes of ovalbumin during denaturation and aggregation by water-soluble carcinogens.
    Biochim Biophys Acta. 1966 Oct 10;126(2):274-85 PMID: 5971853
  14. Protein denaturation.
    Adv Protein Chem. 1968;23:121-282 PMID: 4882248
  15. THE OPTICAL ROTATORY DISPERSION OF SIMPLE POLYPEPTIDES. I.
    Proc Natl Acad Sci U S A. 1956 Sep;42(9):596-603 PMID: 16589913
  16. The formation of the tertiary structure of proteins.
    Harvey Lect. 1967;61:95-116 PMID: 5338078
  17. RENATURATION OF SOLUBLE COLLAGEN. 3. REORGANIZATION OF NATIVE COLLAGEN MOLECULES FROM COMPLETELY SEPARATED UNITS.
    Arch Biochem Biophys. 1964 May;105:387-403 PMID: 14186745
  18. THERMODYNAMIC ANALYSIS OF MULTICOMPONENT SOLUTIONS.
    Adv Protein Chem. 1964;19:287-395 PMID: 14268786
  19. The molecular weights of some crystalline enzymes from muscle and yeast. I. Aldolase and D-glyceraldehyde-3-phosphate dehydrogenase.
    Biochim Biophys Acta. 1956 Apr;20(1):109-14 PMID: 13315356
  20. The denaturation of ovalbumin. Changes in optical rotation, extinction and viscosity during serial denaturation in solutions of urea.
    Biochem J. 1959 Sep;73:86-90 PMID: 13834525
  21. On protein synthesis.
    Symp Soc Exp Biol. 1958;12:138-63 PMID: 13580867
  22. Conformational studies of a series of overlapping peptides from ribonuclease and their relationship to the protein structure.
    Biochemistry. 1969 Jul;8(7):2876-9 PMID: 5817621
  23. On the ionic strength dependence of micelle number. II.
    J Phys Chem. 1967 May;71(6):1898-907 PMID: 6045722
  24. ACHIEVEMENT OF SEDIMENTATION EQUILIBRIUM.
    Proc Natl Acad Sci U S A. 1961 Nov;47(11):1848-52 PMID: 16590906
  25. Evidence for the chemical interaction of urease in solution.
    Biochem J. 1960 Nov;77:230-9 PMID: 13696356
  26. Kinetic aspects of conformational changes in proteins. I. Rate of regain of enzyme activity from denatured proteins.
    Biochemistry. 1971 Mar 2;10(5):792-8 PMID: 5544671
  27. Renaturation of spinach leaf glyoxylic acid reductase.
    J Biol Chem. 1970 Aug 10;245(15):3850-8 PMID: 4321767
  28. Equilibrium and kinetics of the unfolding of lysozyme (muramidase) by guanidine hydrochloride.
    J Mol Biol. 1966 Feb;15(2):489-504 PMID: 5915179
  29. Specificity in the assembly of multisubunit proteins.
    Proc Natl Acad Sci U S A. 1969 Sep;64(1):247-54 PMID: 4904641
  30. The properties of thyroglobulin. XIV. The structure of reoxidized thyroglobulin.
    Biochemistry. 1966 Jul;5(7):2238-45 PMID: 4959961
  31. The reversibility of the denaturation of bacterial luciferase.
    Biochemistry. 1967 Sep;6(9):2893-900 PMID: 6055200
  32. The polymerization of carboxypeptidase A in solutions containing sodium chloride.
    Biochemistry. 1965 Dec;4(12):2691-8 PMID: 5880676
  33. The effects of detergents and urea on the rotatory dispersion of ovalbumin.
    Arch Biochem Biophys. 1962 Nov;99:348-9 PMID: 13935299
  34. Elastase. II. Optical properties and the effects of sodium dodecyl sulfate.
    Biochemistry. 1971 Mar 2;10(5):743-52 PMID: 5544664
  35. Effect of divalent cations on the reduction and re-formation of the disulfide bonds of deoxyribonuclease.
    J Biol Chem. 1969 Feb 10;244(3):929-32 PMID: 4976791
  36. POLYDISPERSE ULTRACENTRIFUGAL PATTERNS OF OVALBUMIN IN PRESENCE OF ALUMINIUM.
    Biochim Biophys Acta. 1963 Nov 29;75:453-5 PMID: 14104959
  37. On the estimation of the shape of macromolecules from sedimentation and viscosity measurements.
    Biochim Biophys Acta. 1965 Jul 22;102(2):549-58 PMID: 5852107
  38. Physicochemical studies on ovalbumin. 3. The sulphydryl and disulphide contents of ovalbumin and an iodine-modified derivative.
    Biochem J. 1962 Jun;83:559-66 PMID: 14007628
  39. THE POLYPEPTIDE CHAINS OF RABBIT GAMMA-GLOBULIN AND ITS PAPAIN-CLEAVED FRAGMENTS.
    Biochemistry. 1964 Feb;3:279-84 PMID: 14163954
  40. On the effect of divalent cations and protein concentration upon renaturation of beta-galactosidase from E. coli.
    Biochem Biophys Res Commun. 1969 Apr 10;35(1):35-42 PMID: 4888537
  41. Subunit structure of hog thyroglobulin: dissociation by treatment with sodium dodecyl sulfate.
    Biochim Biophys Acta. 1969 May;181(1):116-35 PMID: 5792574
  42. Rotatory behavior of protein denaturation.
    Biochim Biophys Acta. 1960 Jan 15;37:336-41 PMID: 13852730
  43. Reduction and reoxidation of the disulfide bonds of bovine serum albumin.
    Arch Biochem Biophys. 1969 Sep;133(2):277-85 PMID: 5387562
  44. Thiol and disulphide contents of hen ovalbumin. C-terminal sequence and location of disulphide bond.
    Biochem J. 1970 Feb;116(4):555-61 PMID: 5435486
  45. An experimental approach to the study of the folding of staphylococcal nuclease.
    J Biol Chem. 1969 Jul 25;244(14):3864-75 PMID: 4308739
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1290665
Published
1972-09-00
Pages
665-76
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1174168
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1290665 PMC Full Text View journal details
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

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2