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Abstract
Human fibroblast interferon preparations were completely stabilized to 100 °C by sodium dodecyl sulphate (SDS) in the presence of mercaptoethanol, but only a minor fraction of their activities were stabilized by SDS without mercaptoethanol. On the contrary, human leukocyte interferon preparations were completely stabilized to 100 °C by SDS in the absence of mercaptoethanol, but only a minor fraction of their activities were stabilized by SDS in the presence of mercaptoethanol.
Furthermore, human fibroblast interferon preparations whose activities had been destroyed by boiling at 100 °C were completely reactivated by SDS under reducing conditions, but only a minor part of their activities were restored by SDS in the absence of reduction. On the contrary, human leukocyte interferon preparations whose activities had been destroyed by boiling at 100 °C were completely reactivated by SDS in the absence of reduction, but only a minor part of their activities were restored by SDS under reducing conditions.
These data suggest that there are distinct molecular species of human interferons.
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