Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1962 Jun;83(3):566–574. doi: 10.1042/bj0830566

Physicochemical studies on ovalbumin. 4. Characterization of an iodine-modified derivative by electrophoresis and sedimentation*

J M Creeth 1, D J Winzor 1,†
PMCID: PMC1243597  PMID: 13882100

Full text

PDF
566

Images in this article

571Fig. 4.
on p.571

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BALDWIN R. L. Boundary spreading in sedimentation-velocity experiments. V. Measurement of the diffusion coefficient of bovine albumin by Fujita's equation. Biochem J. 1957 Mar;65(3):503–512. doi: 10.1042/bj0650503. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BARNETT L. B., BULL H. B. Electrophoresis of ribonuclease and of beta-lactoglobulin: isoelectric points of proteins. Arch Biochem Biophys. 1960 Aug;89:167–172. doi: 10.1016/0003-9861(60)90038-2. [DOI] [PubMed] [Google Scholar]
  3. CREETH J. M., NICHOL L. W. Evidence for the chemical interaction of urease in solution. Biochem J. 1960 Nov;77:230–239. doi: 10.1042/bj0770230. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. CUNNINGHAM L. W., NUENKE B. J. Analysis of modified beta-lactoglobulins and ovalbumins prepared from the sulfenyl iodine intermediates. J Biol Chem. 1960 Jun;235:1711–1715. [PubMed] [Google Scholar]
  5. CUNNINGHAM L. W., NUENKE B. J. Physical and chemical studies of a limited reaction of iodine with proteins. J Biol Chem. 1959 Jun;234(6):1447–1451. [PubMed] [Google Scholar]
  6. Charlwood P. A. The valences of protein ions from electrophoretic and membrane potential measurements. Biochem J. 1950 Mar;46(3):312–319. doi: 10.1042/bj0460312. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. FOSTER J. F., RHEES R. C. An investigation by light scattering of aggregation in the heat denaturation of ovalbumin. Arch Biochem Biophys. 1952 Oct;40(2):437–447. doi: 10.1016/0003-9861(52)90131-8. [DOI] [PubMed] [Google Scholar]
  8. FRAENKEL-CONRAT H. The reaction of tobacco mosaic virus with iodine. J Biol Chem. 1955 Nov;217(1):373–381. [PubMed] [Google Scholar]
  9. MACLAREN J. A., LEACH S. J., O'DONNELL I. J. The oxidation of disulphide groups in proteins. Biochim Biophys Acta. 1959 Sep;35:280–281. doi: 10.1016/0006-3002(59)90371-3. [DOI] [PubMed] [Google Scholar]
  10. MILLER G. L., GOLDER R. H. Sedimentation studies with the Spinco ultracentrifuge. Arch Biochem Biophys. 1952 Apr;36(2):249–258. doi: 10.1016/0003-9861(52)90409-8. [DOI] [PubMed] [Google Scholar]
  11. PERLMANN G. E. Enzymatic dephosphorylation of ovalbumin and plakalbumin. J Gen Physiol. 1952 May;35(5):711–726. doi: 10.1085/jgp.35.5.711. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. WALDMANN-MEYER H. Thermodynamic proton-, cadmium-, and zinc-binding constants of serum albumin determined by zone electrophoresis. J Biol Chem. 1960 Nov;235:3337–3345. [PubMed] [Google Scholar]
  13. WINZOR D. J., CREETH J. M. Physicochemical studies on ovalbumin. 3. The sulphydryl and disulphide contents of ovalbumin and an iodine-modified derivative. Biochem J. 1962 Jun;83:559–566. doi: 10.1042/bj0830559. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES