Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1975 Jun;147(3):613–615. doi: 10.1042/bj1470613

Hydrodynamic changes accompanying the loss of metal ions from concanavalin A.

H W Sawyer, R Dabscheck, P R Nott, B K Selinger, I D Kuntz
PMCID: PMC1165490  PMID: 241332

Abstract

The hydrodynamic changes which accompany the dissociation of metal ions, from concanavalin A at acid pH are a result of charge effects rather than of dissociation of metal ions as such. Measurements of the rotational relaxation time are discussed in terms of the hydration of the protein and its polymeric heterogeneity.

Full text

PDF
613

Selected References

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

  1. Agrawal B. B., Goldstein I. J. Protein-carbohydrate interaction. VI. Isolation of concanavalin A by specific adsorption on cross-linked dextran gels. Biochim Biophys Acta. 1967 Oct 23;147(2):262–271. [PubMed] [Google Scholar]
  2. Chen R. F. Dansyl labeled proteins: determination of extinction coefficienc and number of bound residues with radioactive dansyl chloride. Anal Biochem. 1968 Oct 24;25(1):412–416. doi: 10.1016/0003-2697(68)90116-4. [DOI] [PubMed] [Google Scholar]
  3. Edelman G. M., Cunningham B. A., Reeke G. N., Jr, Becker J. W., Waxdal M. J., Wang J. L. The covalent and three-dimensional structure of concanavalin A. Proc Natl Acad Sci U S A. 1972 Sep;69(9):2580–2584. doi: 10.1073/pnas.69.9.2580. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hardman K. D., Ainsworth C. F. Structure of concanavalin A at 2.4-A resolution. Biochemistry. 1972 Dec 19;11(26):4910–4919. doi: 10.1021/bi00776a006. [DOI] [PubMed] [Google Scholar]
  5. Hassing G. S., Goldstein I. J. Ultraviolet difference spectral studies on concanavalin A. Carbohydrate interaction. Eur J Biochem. 1970 Nov;16(3):549–556. doi: 10.1111/j.1432-1033.1970.tb01116.x. [DOI] [PubMed] [Google Scholar]
  6. Inbar M., Shinitzky M., Sachs L. Rotational relaxation time of concanavalin A bound to the surface membrane of normal and malignant transformed cells. J Mol Biol. 1973 Dec 5;81(2):245–253. doi: 10.1016/0022-2836(73)90192-7. [DOI] [PubMed] [Google Scholar]
  7. Kuntz I. D. Hydration of macromolecules. IV. Polypeptide conformation in frozen solutions. J Am Chem Soc. 1971 Jan 27;93(2):516–518. doi: 10.1021/ja00731a037. [DOI] [PubMed] [Google Scholar]
  8. Kuntz I. D., Jr, Kauzmann W. Hydration of proteins and polypeptides. Adv Protein Chem. 1974;28:239–345. doi: 10.1016/s0065-3233(08)60232-6. [DOI] [PubMed] [Google Scholar]
  9. McKenzie G. H., Sawyer W. H., Nichol L. W. The molecular weight and stability of concanavalin A. Biochim Biophys Acta. 1972 Apr 15;263(2):283–293. doi: 10.1016/0005-2795(72)90081-5. [DOI] [PubMed] [Google Scholar]
  10. Pflumm M. N., Wang J. L., Edelman G. M. Conformational changes in concanavalin A. J Biol Chem. 1971 Jul 10;246(13):4369–4370. [PubMed] [Google Scholar]
  11. Sawyer W. H., McKenzie G. H., Nichol L. W. A conformational transition in concanavalin A. Conformational differences between intact and fragmented units. Aust J Biol Sci. 1974 Feb;27(1):1–6. [PubMed] [Google Scholar]
  12. Yang D. C., Gall W. E., Edelman G. M. Rotational correlation time of concanavalin A after interaction with a fluorescent probe. J Biol Chem. 1974 Nov 10;249(21):7018–7023. [PubMed] [Google Scholar]

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

RESOURCES