Abstract
It has been shown previously that those samples of human albumin which, when freshly isolated using an ethanolic solution of hydrochloric acid, were antagonistic towards insulin lost their activity if stored for a period in air. To eliminate the possibility that antagonist was an artefact of the isolation procedure, samples of air-stored albumins were dissolved in water and subjected to re-extraction using an ethanolic solution of hydrochloric acid. Antagonistic activity was not regenerated. The storage characteristics of albumin isolated by trichloroacetic acid were also studied. It was found that samples stored in air for a period before bioassay were devoid of antagonism. This finding provides a possible explanation for the conflicting results obtained in some previous studies on synalbumin.
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