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Molecular Pharmacology, Vol 15, 685-690, Copyright © 1979 by the American Society for Pharmacology and Experimental Therapeutics
1 Roswell Park Memorial Institute, Buffalo, New York 14263
2 HEM Research, Rockville, Maryland 20852
Interferon derived from a lower animal source, porcine leukocytes, is shown to have high biological activity in human cell cultures. This interferon shares some biochemical properties with human leukocyte interferon which had been shown previously to protect cells of animal origin. For example, when chromatographed on Phenyl-Sepharose CL-4B, both porcine and human leukocyte interferons bound and could be eluted with 50% ethylene glycol. Similarly, both porcine and human leukocyte interferons did not bind under physiological salt and pH conditions to concanavalin A-agarose. In contrast, the interferon produced by a variety of human and lower animal fibroblastswhich display much reduced cross-species activityinteract strongly with this lectin. Presumably, due to altered glycosylation, leukocyte interferons more easily express cross-species activity.
It seems that, generally, interferons elaborated by leukocytes are less restrictive in their species specificity than those elaborated by fibroblasts. Our findings suggest a possible structural homology between human leukocyte and porcine leukocyte interferons similar to those well recognized between various polypeptide hormones of animal and human origin.
Submitted on August 1, 1978