Literature DB >> 5492846

Thermal denaturation of human haemoglobins.

J Kinderlerer, H Lehmann, K F Tipton.   

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Year:  1970        PMID： 5492846      PMCID： PMC1179552          DOI： 10.1042/bj1190066pc

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


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  3 in total

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2.  Qualitative and quantitative studies of sickle cell hemoglobin in homozygotes and heterozygotes.

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3.  Reversible denaturation of sperm whale myoglobin. I. Dependence on temperature, pH, and composition.

Authors:  G Acampora; J Hermans
Journal:  J Am Chem Soc       Date:  1967-03-29       Impact factor: 15.419
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1.  Circular dichroism spectra of human hemoglobin reveal a reversible structural transition at body temperature.

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2.  Body temperature-related structural transitions of monotremal and human hemoglobin.

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3.  Differential thermal stability and oxidative vulnerability of the hemoglobin variants, HbA2 and HbE.

Authors:  Abhijit Chakrabarti; Dipankar Bhattacharya; Sanghamitra Deb; Madhumita Chakraborty
Journal:  PLoS One       Date:  2013-11-14       Impact factor: 3.240
  3 in total

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