文章基本信息

标题：Interferon: Evidence for Its Glycoprotein Nature
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作者：F. Dorner ; M. Scriba ; R. Weil 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1973
卷号：70
期号：7
页码：1981-1985
DOI：10.1073/pnas.70.7.1981
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：In an attempt to understand the structure of rabbit interferon, the possibility of carbohydrate being part of the molecule was tested. Interferon incubated with neuraminidase from Vibrio cholera is homogeneous in charge as revealed by isoelectric focusing. Treatment of "asialointerferon" with galactose oxidase (EC 1.1.3.9 ) from Dactylium dendroides and subsequent reduction with tritiated sodium borohydride yields labeled material with unimpaired antiviral activity. Enzymic incorporation of N-[14C]acetylneuraminic acid into tritiated asialointerferon restores the original charge heterogeneity. The newly generated sialointerferon contains both 3H and 14C activity. Asialointerferon is retained by an affinity column containing phytohemagglutinin from Phaseolus vulgaris and can be displaced from the adsorbent by a glycoprotein of known structure. It is concluded that rabbit interferon is a glycoprotein containing the terminal oligosaccharide sequence sialic acid [->] galactose.
关键词：sialic acid ; galactose ; phytoagglutinin ; affinity chromatography