Literature DB >> 884202

Resolvability of Adair constants from oxygenation curves measured at low hemoglobin concentration.

M L Johnson, G K Ackers.   

Abstract

Analyses of low concentration oxygenation curves for apparent Adair constants in which the effects of dimers is ignored have been explored using recently determined values of the overall energy coupling parameters. For high affinity systems and favorable energy distributions, it is found that the errors in estimated binding free energies may be less than one kcal provided the measurement errors are strictly random and of small magnitude. These errors are nevertheless quite substantial as compared with the differences between values for the successive binding steps.

Mesh:

Substances:

Year:  1977        PMID: 884202     DOI: 10.1016/0301-4622(77)87017-8

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  3 in total

1.  Reciprocal effects in human hemoglobin: direct measurement of the dimer-tetramer association constant at partial oxygen saturation.

Authors:  R Valdes; L P Vickers; H R Halvorson; G K Ackers
Journal:  Proc Natl Acad Sci U S A       Date:  1978-11       Impact factor: 11.205

2.  Evaluation and propagation of confidence intervals in nonlinear, asymmetrical variance spaces. Analysis of ligand-binding data.

Authors:  M L Johnson
Journal:  Biophys J       Date:  1983-10       Impact factor: 4.033

3.  Energetics of subunit assembly and ligand binding in human hemoglobin.

Authors:  G K Ackers
Journal:  Biophys J       Date:  1980-10       Impact factor: 4.033

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.