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1.
Comparison of the applicability of several allosteric models to the pH and 2,3-bis(phospho)glycerate dependence of oxygen binding by human blood.
El-Yassin, D I; Fell, D A.
J Mol Biol ; 156(4): 863-89, 1982 Apr 25.
Article in English | MEDLINE | ID: mdl-7120397

Subject(s)
Diphosphoglyceric Acids/blood , Models, Biological , Oxygen/blood , Oxyhemoglobins/metabolism , 2,3-Diphosphoglycerate , Allosteric Site , Computers , Humans , Hydrogen-Ion Concentration
2.
The breakdown of 2,3-bis(phospho)-D-glycerate by Fe(III)-haemoglobin.
El-Yassin, D I; Fell, D A; Lloyd, B B; Fisher, R B.
Biochem J ; 177(1): 373-5, 1979 Jan 01.
Article in English | MEDLINE | ID: mdl-426777

ABSTRACT

Fe(III)-haemoglobin is shown to catalyse the hydrolysis of 2,3-bis(phospho)-D-glycerate to Pi and 3-phosphoglycerate, although the rate is slow, even when the protein is present at concentrations in the millimolar range. The rate of hydrolysis is proportional to the subtrate concentration up to at least 10 mM, so if the process is enzymic, the Km must be high.


Subject(s)
Diphosphoglyceric Acids/blood , Hemoglobins/metabolism , Ferric Compounds/metabolism , Humans , Kinetics
3.
An automated mixing apparatus for determining haemoglobin-oxygen dissociation [proceedings].
El-Yassin, D I; Fell, D A; Lloyd, B B; Seaton, B.
J Physiol ; 282: 3P-4P, 1978 Sep.
Article in English | MEDLINE | ID: mdl-31462

Subject(s)
Hematology/instrumentation , Oxygen/blood , Carbon Dioxide/blood , Hemoglobins/metabolism , Hydrogen-Ion Concentration
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