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A Novel Peptide with ribonuclease and translation-inhibitory activities from fruiting bodies of the oyster mushroom Pleurotus ostreatus

✍ Scribed by X. Y. Ye; T. B. Ng


Publisher
John Wiley and Sons
Year
2002
Tongue
English
Weight
134 KB
Volume
8
Category
Article
ISSN
1075-2617

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✦ Synopsis


Abstract

From the fresh fruiting bodies of the oyster mushroom a peptide with a molecular weight of 9 kDa and demonstrating a novel N‐terminal sequence GPCYLVAFYESSGRR was isolated. The isolation procedure involved ion exchange chromatography on CM‐Sepharose and Mono S. The peptide was adsorbed on both types of chromatographic media. The peptide demonstrated a ribonuclease activity of 650 U/mg toward yeast transfer RNA. It inhibited cell‐free translation in a rabbit reticulocyte lysate system with an IC~50~ of 15 nM. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.


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Purification and characterization of a n
✍ X. Y. Ye; Dr T. B. Ng 📂 Article 📅 2003 🏛 John Wiley and Sons 🌐 English ⚖ 93 KB

## Abstract A ribonuclease (RNase), possessing an __N__‐terminal sequence disparate from those of ribonucleases from other mushrooms and previously isolated __Pleurotus ostreatus__ RNases, was purified from the fruiting bodies of the edible mushroom __Pleurotus ostreatus__. The __N__‐terminal seque