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, beta-glucosidase and beta-glucuronidase. Its N-terminal sequence exhibited a certain degree of similarity to those of plant ribosome inactivating proteins.
journal_name
Life Scijournal_title
Life sciencesauthors
Wang H,Ng TBdoi
10.1016/s0024-3205(01)01023-2subject
Has Abstractpub_date
2001-03-23 00:00:00pages
2151-8issue
18eissn
0024-3205issn
1879-0631pii
S0024320501010232journal_volume
68pub_type
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