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Purification and characterization of a lectin from the mushroom, Flammulina veltipes.

作者信息

Tsuda M

出版信息

J Biochem. 1979 Nov;86(5):1463-8. doi: 10.1093/oxfordjournals.jbchem.a132664.

Abstract

A lectin was purified to homogeneity from the mushroom, Flammulina veltipes, by zinc acetate treatment and CM-cellulose column chromatography. Its molecular weight was estimated to be 20,000 by gel filtration and polyacrylamide gel electrophoresis. The lectin does not contain carbohydrate, half-cystine, methionine, or histidine. On gel filtration sith Sepharose 6B in the presence of 6M guanidine-HCl, the purified lectin dissociated into two nonidentical subunits, FVA-L (molecular weight, 12,000) and FVA-S (8,000). The hemagglutinating activity was retained only in the FVA-L subunit. The lectin is mitogenic with respect to mouse spleen lymphocytes.

摘要

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