Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/18688
Title: Purification and characterization of a ribonuclease from the wild edible mushroom Armillaria luteo-virens
Authors: Xu, Li-Jing
Chen, Qing-Jun
Wang, He-Xiang
Zhang, Guo-Qing
Keywords: Armillaria luteo-virens;Muchroom;Purification;Ribonuclease
Issue Date: Jun-2013
Publisher: NISCAIR-CSIR, India
Abstract: A 15 kDa ribonuclease (RNase) was purified from dried fruiting bodies of the wild edible mushroom Armillaria luteo-virens. The simple 4-step purification protocol involved ion-exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion-exchange chromatography on SP-Sepharose and a final gel filtration by FPLC on Superdex-75. The RNase was unadsorbed on Affi-gel blue gel, but adsorbed on DEAE-cellulose and SP-Sepharose. The N-terminal amino acid sequence of purified RNase was AGVQYKLTILLV, which showed low sequence homology to those of previously reported RNases. The optimal pH and temperature of the enzyme were very close to 4.0 and 70°C, respectively. The enzyme showed considerably high ribonucleolytic activity and broad specificity towards polyhomoribonucleotides, with a specificity of poly(U)>poly(C)>poly (G)>poly(A). The ribonucleolytic activities towards poly(U), poly(C), poly(G) and poly(A) were 279.5, 184.1, 69.9 and 52.3 U/mg, respectively.
Page(s): 196-201
URI: http://hdl.handle.net/123456789/18688
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.50(3) [June 2013]

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