| Literature DB >> 574868 |
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.Entities:
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Year: 1979 PMID: 574868 DOI: 10.1093/oxfordjournals.jbchem.a132664
Source DB: PubMed Journal: J Biochem ISSN: 0021-924X Impact factor: 3.387