20 research outputs found
The Effect of DPG and IHP on the Relative Thermodynamic Affinity for CO of the Subunits of Rabbit Hemoglobin
The two chains of most hemoglobins interact
differently with ligands as can be seen in two
nmr resonances for bound ^(13)CO (Moon and
Richards, 1972). This observation has led to interest
in the possibility that the two chains have
different thermodynamic affinities toward ligands
(Huestis and Raftery, 1973, 1975; Moon and
Richards, 1974; Huang and Redfield, 1976;
Viggiano and Ho, 1979a,b).
Rabbit hemoglobin possesses an unusual α-chain
which causes ^(13)CO bound to it to have a
different chemical shift than ^(13)CO bound to β chains (Moon and Richards, 1972, 1974) and,
thereby, allows direct quantitative observation of
the degree of ligation of the two subunits
Competition and oligopoly in the context of the UK and German steel industries Forecasting the demand for UK steel
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