Literature DB >> 3390529

On the determination of species fractions from ligand-binding data. Application to human hemoglobin.

E Di Cera1, S J Gill.   

Abstract

A method outlined in a previous study (S.J. Gill, H.T. Gaud, J. Wyman and G. Barisas, Biophys. Chem. 8 (1978) 53) is applied for the determination of species fractions from ligand-binding data for the oxygen reaction with human hemoglobin. The results obtained by this alternative approach, which is based on the solution of a system of linear equations, are consistent with those obtained using nonlinear least-squares analysis.

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Year:  1988        PMID： 3390529     DOI： 10.1016/0301-4622(88)85057-9

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


  4 in total

1.  Allosteric equilibria in the binding of fibrinogen to platelets.

Authors:  R De Cristofaro; R Landolfi; E De Candia; M Castagnola; E Di Cera; J Wyman
Journal:  Proc Natl Acad Sci U S A       Date:  1988-11       Impact factor: 11.205

2.  Temperature- and pH-dependence of the oxygen-binding reaction of human fetal haemoglobin.

Authors:  M L Doyle; S J Gill; R De Cristofaro; M Castagnola; E Di Cera
Journal:  Biochem J       Date:  1989-06-01       Impact factor: 3.857

3.  Free energy changes and components implicit in the MWC allosteric model for the cooperative oxygen binding of hemoglobin.

Authors:  Enrico Bucci; Stefania Pucciarelli; Mauro Angeletti
Journal:  Biochemistry       Date:  2013-06-10       Impact factor: 3.162

4.  Recombinant human hemoglobin: expression and refolding of beta-globin from Escherichia coli.

Authors:  C Fronticelli; J K O'Donnell; W S Brinigar
Journal:  J Protein Chem       Date:  1991-10
  4 in total

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