Literature DB >> 19872790

THE EQUILIBRIA BETWEEN NATIVE AND DENATURED HEMOGLOBIN IN SALICYLATE SOLUTIONS AND THE THEORETICAL CONSEQUENCES OF THE EQUILIBRIUM BETWEEN NATIVE AND DENATURED PROTEIN.

M L Anson1, A E Mirsky.   

Abstract

The denaturation of hemoglobin by salicylate in neutral solution is completely reversible. There is a mobile equilibrium between native and denatured hemoglobin in neutral salicylate solution. The higher the salicylate concentration the greater is the percentage denaturation. When there is a mobile equilibrium between the native and denatured forms of a protein, denaturation is caused by the addition of any substance which has a greater affinity for the denatured than for the native form. Theoretically the heat of denaturation must vary with the denaturing agent and must depend on the heat of combination of the denaturing agent with the protein.

Entities:  

Year:  1934        PMID: 19872790      PMCID: PMC2141288          DOI: 10.1085/jgp.17.3.399

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


  2 in total

Review 1.  Enzymes, drugs and antibodies, some chemical common factors.

Authors:  J H Turnbull
Journal:  Experientia       Date:  1964-03-15

2.  Hydrophobic-hydrophilic forces in protein folding.

Authors:  Stewart R Durell; Arieh Ben-Naim
Journal:  Biopolymers       Date:  2017-08       Impact factor: 2.505

  2 in total

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