Collect. Czech. Chem. Commun.
1981, 46, 1288-1295
https://doi.org/10.1135/cccc19811288
The conformational changes of haemoglobin on its binding to haptoglobin
Barbora Dvořánková and Zdeněk Pavlíček
Department of Physical Chemistry, Charles University, 128 40 Prague 2
Abstract
The binding of human haemoglobin to human haptoglobin has been found to alter the conformation of haemoglobin. Spectrophotometric measurements, measuring of peroxidase activity, thin-layer gel chromatography and modelling on an analogue computer led to the conclusion that the binding of haemoglobin to haptoglobin was associated with a change in the quaternary structure of haemoglobin, with a transition from the R state to the T state. The kinetics of the conformational changes had an autocatalytic character.
