Isolation and characterization of velutin, a novel low-molecular-weight ribosome-inactivating protein from winter mushroom (Flammulina velutipes) fruiting bodies.

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 Sci

journal_title

Life sciences

authors

Wang H,Ng TB

doi

10.1016/s0024-3205(01)01023-2

subject

Has Abstract

pub_date

2001-03-23 00:00:00

pages

2151-8

issue

18

eissn

0024-3205

issn

1879-0631

pii

S0024320501010232

journal_volume

68

pub_type

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