Abstract
The influence of link-glycoproteins and mammalian lysozyme on the configuration and size of the hyaluronate molecule in highly diluted solutions under physiological electrolytic and pH conditions was investigated by light-scattering techniques and confirmed by column chromatography, isopycnic flotation, and boundary centrifugation. It was consistently found that link-glycoproteins induce an increase in the basic structural dimensions of the hyaluronate molecule in solution. It was also found that this increase was reversed or prevented under the action of mammalian lysozyme. Changes in configuration of the hyaluronate molecule could be related to its aggregating capacity when the hyaluronate interacts with proteoglycan subunits. It is postulated that link-glycoproteins induce structural changes in the hyaluronate molecule that might improve its aggregating capacity while mammalian lysozyme prevents or regulates such improvement.
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