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A novel and potent ribonuclease from fruiting bodies of the mushroom Pleurotus pulmonarius.

Abstract：

:A ribonuclease (RNase), with an N-terminal sequence different from those of ribonucleases from the mushrooms Irpex lacteus, Lentinus edodes, Pleurotus ostreatus, Pleurotus tuber-regium, and Volvariella volvacea, was purified from fruiting bodies of the edible mushroom Pleurotus pulmonarius. The N-terminal sequence of P. pulmonarius RNase manifested homology to a portion of the sequences of ribosome inactivating protein abrin-b, abrin-c, and abrin-d, and Bacillus subtilis transcriptional regulator. The ribonuclease was adsorbed on Affi-gel blue gel, CM-Sepharose, and Mono S. It displayed a molecular mass of 14.4 kDa in both sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration on Superdex 75. The ribonuclease exhibited an activity of 25 114 U/mg on yeast tRNA. The highest ribonucleolytic activity was demonstrated toward poly C, followed by poly A, and then by poly G. There was no activity toward poly U. The optimal pH for its activity was 7 and the optimal temperature was 55 degrees C. It inhibited cell-free translation in a rabbit reticulocyte lysate with an IC50 of 0.33 nM.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Ye XY,Ng TB

doi

10.1016/S0006-291X(02)00301-7

subject

Has Abstract

pub_date

2002-05-03 00:00:00

pages

857-61

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(02)00301-7

journal_volume

293

pub_type

杂志文章

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