Literature DB >> 19872217

STUDIES IN THE PHYSICAL CHEMISTRY OF THE PROTEINS : VI. THE ACTIVITY COEFFICIENTS OF THE IONS IN CERTAIN OXYHEMOGLOBIN SOLUTIONS.

E J Cohn1, A M Prentiss.   

Abstract

1. The solvent action of a neutral salt upon a protein, oxyhemoglobin, has been found identical to the solvent action of a neutral salt upon a bi-bivalent or uni-quadrivalent compound. 2. The solubility of oxyhemoglobin in phosphate solutions of varying ionic strength has been defined by the equation: log See PDF for Equation in which micro is the ionic strength, and S(0) is the solubility in the absence of salt. 3. The values of S(0) have been calculated to be 12.2, 11.2, and 13.1 gm. per liter respectively at pH 6.4, 6.6, and 6.8. 4. The relatively great solubility of oxyhemoglobin in water has been ascribed to the strong affinity constants for acid and base of certain groups in oxyhemoglobin. 5. The small change in the solubility of oxyhemoglobin effected by neutral salts suggests that but few such groups are dissociated in oxyhemoglobin in the state in which it crystallizes near its isoelectric point. 6. Certain of the other properties of oxyhemoglobin, such as its low viscosity, are considered in the light of its molecular weight and its valence type.

Entities:  

Year:  1927        PMID: 19872217      PMCID: PMC2140815          DOI: 10.1085/jgp.8.6.619

Source DB:  PubMed          Journal:  J Gen Physiol        ISSN: 0022-1295            Impact factor:   4.086


  1 in total

1.  The Viscosity and Hydratation of Colloidal Solutions.

Authors:  E Hatschek
Journal:  Biochem J       Date:  1916-10       Impact factor: 3.857

  1 in total
  1 in total

1.  GRPY: An Accurate Bead Method for Calculation of Hydrodynamic Properties of Rigid Biomacromolecules.

Authors:  Pawel J Zuk; Bogdan Cichocki; Piotr Szymczak
Journal:  Biophys J       Date:  2018-07-24       Impact factor: 4.033

  1 in total

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