Abstract
A glycoprotein, with a ubiquitin-like N-terminal sequence, has been prepared from an extract of fruiting bodies of the mushroom Pleurotus ostreatus, using a procedure which included ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on SP-Sepharose and Mono Q and gel filtration on Superdex 75. It exhibited a molecular weight of 12.5 kDa and was unadsorbed on DEAE-cellulose and Mono Q, but adsorbed on Affi-blue gel and SP-Sepharose. It inhibited translation in a rabbit reticulocyte lysate system (IC50 = 160 nM) and exhibited low ribonucleolytic activity (14 μ/mg) toward yeast tRNA. It also expressed an inhibitory activity toward human immunodeficiency virus-1 reverse transcriptase, which could be enhanced by succinylation.
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