Models for hemoglobin and allosteric enzymes

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Abstract
A model for hemoglobin is proposed and its application to allosteric enzymes is discussed with particular reference to asparate transcarbamylase. The main assumptions made are that the molecule is composed of subunits and that occupation of a sub‐unit produces a conformational change which affects the occupational probability of neighboring subunits. The results compare favorably with experiment and a number of specific predictions are made for aspartate transcarbamylase.
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