Abstract
The solubility of polymers formed by haemoglobins with one βs chain and one mutant α chain, either cis or trans to each other, has revealed three distinct regions on the surface of the tetramer which participate in intermodular bonding within the haemoglobin S fibre.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Wishner, B. C., Ward, K. B., Lattman, E. E. & Love, W. E. J. molec. Biol. 98, 179–194 (1975).
Magdoff-Fairchild, B. & Chiu, C. C. Proc. natn. Acad. Sci. U.S.A. 76, 223–226 (1979).
Wellems, T. E., Vasser, R. J. & Josephs, R. J. molec. Biol. 153, 1011–1026 (1981).
Pumphrey, J. G. & Steinhardt, J. Biochem. biophys. Res. Commun. 69, 929–931 (1976).
Pumphrey, J. G. & Steinhardt, J. J. molec. Biol. 112, 359–375 (1977).
Benesch, R. E., Yung, S., Benesch, R., Mack, J. & Schneider, R. G. Nature 260, 219–221 (1976).
Benesch, R. E., Kwong, S., Benesch, R. & Edalji, R. Nature 269, 772–775 (1977).
Benesch, R., Kwong, S., Benesch, R. E. & Edalji, R. INSERM Symp. on Molecular Interactions of Hemoglobin 70, 221–230 (1977).
Nagel, R. L. et al. Nature 283, 832–834 (1980).
Dykes, G. E., Crepeau, R. H. & Edelstein, S. J. J. molec. Biol., 130, 451–472 (1979).
Crepeau, R. H. et al. Proc. natn. Acad. Sci. U.S.A. 78, 1406–1410 (1981).
Bookchin, R. M. & Nagel, R. L. J. molec. biol. 60, 263–270 (1971).
Bookchin, R. M., Balazs, T., Nagel, R. L. & Tellez, I. Nature 269, 526–527 (1977).
Benesch, R. E., Benesch, R., Edalji, R. & Kwong, S. Biochem. biophys. Res. Commun. 81, 1307–1312 (1978).
Josephs, R., Jarosch, H. S. & Edelstein, S. J. J. molec. Biol. 102, 409–426 (1976).
Edelstein, S. J. J. molec. Biol. 150, 557–575 (1981).
Edelstein, S. J. Texas Rep. Biol. Med. 40, 221–232 (1981).
Wellems, T. E. & Josephs, R. J. molec. Biol. 137, 443–450 (1980).
Benesch, R., Benesch, R. E., Yung, S. & Edalji, R. Biochem. biophys. Res. Commun. 63, 1123–1129 (1975).
Benesch, R. E. & Benesch, R. Meth. Enzym. 76, 147–159 (1981).
Arnone, A., Benesch, R. E. & Benesch, R. J. molec. Biol. 115, 627–642 (1977).
Acharya, A. S. & Manning, J. M. J. biol. Chem. 225, 1406–1412 (1980).
Benesch, R. E., Benesch, R., Renthal, R. D. & Maeda, N. Biochemistry 11, 3576–3582 (1972).
Abraham, E. C., Reese, A., Stallings, M. & Huisman, T. H. Haemoglobin 1, 27–44 (1976).
Benesch, R. E., Kwong, S., Edalji, R. & Benesch, R. J. biol. Chem. 254, 8169–8172 (1979).
Benesch, R. E., Edalji, R., Benesch, R. & Kwong, S. Proc. natn. Acad. Sci. U.S.A. 77, 5130–5134 (1980).
Ross, P. D., Briehl, R. W. & Minton, A. P. Biopolymers 17, 2285–2288 (1978).
Macleod, R. M. & Hill, R. J. J. biol. Chem. 248, 100–103 (1973).
Benesch, R., Macduff, G. & Benesch, R. E. Analyt. Biochem. 11, 81–87 (1965).
Benesch, R. E., Benesch, R. & Yung, S. Analyt. Biochem. 55, 245–248 (1973).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Benesch, R., Kwong, S. & Benesch, R. The effects of α chain mutations cis and trans to the β6 mutation on the polymerization of sickle cell haemoglobin. Nature 299, 231–234 (1982). https://doi.org/10.1038/299231a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/299231a0
This article is cited by
-
Modification of Axial Fiber Contact Residues Impact Sickle Hemoglobin Polymerization by Perturbing a Network of Coupled Interactions
The Protein Journal (2007)
-
Reductive hydroxyethylation of the α-amino groups of amidated hemoglobin S
Journal of Protein Chemistry (1985)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.