The effects of salts on the subunit structure and dissociation of Lumbricus terrestris hemoglobin.

Biochemistry
J P Harrington, T T Herskovits

Abstract

The effects of the neutral salts of the Hofmeister series, NaCl, NaClO4, MgCl2, NaI, and also guanidine hydrochloride (Gdn-HCl)on the subunit organization and the state of association of Lumbricus terrestris hemoglobin were examined by light scattering molecular weight measurements. The subunit dissociation of the parent duodecameric structure of 3 x 10(6) molecular weight by various salts is similar in pattern to the sequential splitting of the associated protein to half-molecules of hexamers of 1.5 x 10(6) molecular weight, followed by further dissociation at higher reagent concentration to monomers of 250000 molecular weight. Duodecamer to hexamer dissociation is observed in 0.4 M MgCl2, 1-2 M NaCl, and 1 M Gdn-HCl, while hexamer to monomer dissociation is seen in the presence of 1 M MgCl2. All three species of duodecamers, hexamers, and monomers seem to be present in 1 M NaClO4. Further splitting of the monomers of A subunits to smaller B fragments of one-third to one-quarter molecular weight is observed in 1 M NaI solutions. Optical rotation in the peptide region and absorption measurements in the Soret region indicate the salt dissociation of Lumbricus terrestris hemoglobin is not accompanied by major changes in the foldi...Continue Reading

Citations

May 27, 1977·Biochimica Et Biophysica Acta·S N VinogradovH Mizukami
Jan 1, 1979·Progress in Biophysics and Molecular Biology·M C Chung, H D Ellerton
Apr 13, 1994·Biochimica Et Biophysica Acta·R E HirschJ P Harrington
Jan 1, 1988·Comparative Biochemistry and Physiology. A, Comparative Physiology·G PolidoriS N Vinogradov
Jan 1, 1987·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·T A BorgeseR L Nagel
Nov 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·S N VinogradovA V Crewe
Sep 22, 2015·The Journal of Physical Chemistry. B·Thomas M Scherer
Aug 1, 1987·International Journal of Peptide and Protein Research·R Bhat, J C Ahluwalia
Dec 19, 1996·Chemical Reviews·Jean N. LamySerge N. Vinogradov

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