Literature DB >> 240418

Hemoglobin Cochin-Port-Royal: consequences of the replacement of the beta chain C-terminal by an arginine.

H Wajcman, J V Kilmartin, A Najman, D Labie.   

Abstract

Hemoglobin Cochin Port-Royal beta 146 (HC3) His yields Arg is the second example in which the beta C-terminal residue is replaced. Owing to the known importance of His beta 146 in the co-operative effects of hemoglobin, the functional properties of this variant were carefully studied. It had a normal Hill coefficient but a reduced alkaline Bohr effect. However, the reduction in Bohr effect is less than the halving predicted from previous mutants and modified hemoglobins.

Entities:  

Mesh:

Substances:

Year:  1975        PMID: 240418     DOI: 10.1016/0005-2795(75)90191-9

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Structure-specific model of hemoglobin cooperativity.

Authors:  A W Lee; M Karplus
Journal:  Proc Natl Acad Sci U S A       Date:  1983-12       Impact factor: 11.205

2.  Lack of conventional oxygen-linked proton and anion binding sites does not impair allosteric regulation of oxygen binding in dwarf caiman hemoglobin.

Authors:  Roy E Weber; Angela Fago; Hans Malte; Jay F Storz; Thomas A Gorr
Journal:  Am J Physiol Regul Integr Comp Physiol       Date:  2013-05-29       Impact factor: 3.619

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.