Abstract
From the fruiting bodies of the edible mushroom Flammulina velutipes a single-chained ribosome inactivating protein with a molecular weight of 13.8 kDa was isolated with a procedure involving ion exchange chromatography on DEAE-cellulose and SP-Sepharose and affinity chromatography on Affi-gel blue gel. The protein was novel in that it possessed a molecular weight lower than those of previously reported RIPs and that it was capable of inhibiting human immunodeficiency virus (HIV-1) reverse transcriptase, β-glucosidase and β-glucuronidase. Its N-terminal sequence exhibited a certain degree of similarity to those of plant ribosome inactivating proteins.
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