These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: The thermal denaturation of human oxyhaemoglobins A, A2, C and S.
    Author: Kinderlerer J, Lehmann H, Tipton KF.
    Journal: Biochem J; 1973 Dec; 135(4):805-14. PubMed ID: 4778277.
    Abstract:
    1. The time-courses of thermal denaturation of human oxyhaemoglobins A, A(2), C and S at 45 degrees C were studied by following the increase in protein fluorescence. Haemoglobins S and C were less stable than haemoglobin A, whereas haemoglobin A(2) was considerably more stable. 2. The time-courses of denaturation did not follow first-order kinetics and could be fitted most simply to a co-operative scheme in which the partial denaturation of the alpha chain preceded that of the beta chain. 3. The denaturation of these haemoglobins was studied as a function of temperature by using optical rotatory dispersion. Haemoglobin A(2) was again more stable than the others. The addition of small quantities of haemoglobin A(2) had a disproportionate effect on the stability of haemoglobin C. 4. The thermodynamic parameters of the denaturation process were calculated.
    [Abstract] [Full Text] [Related] [New Search]