Biochemical characterization of the RNA-hydrolytic activity of a pumpkin 2S albumin.

Abstract:

:A pumpkin 2S albumin with ribonuclease (RNase) activity was purified from pumpkin seeds (Cucurbita sp.) by liquid chromatographic techniques. It manifested potent RNase activity toward baker's yeast RNA and calf liver RNA, and some polyhomoribonucleotides, including poly(A), poly(U) and poly(C) but not poly(G). Moreover, it was able to hydrolyze total RNA of both animal and plant origins. Ions such as Na(+), Mg(2+), Ca(2+), and Zn(2+) inhibited its RNase activity. Since RNase activity has not been previously reported in 2S albumins, this work may shed further light on the biological importance of this group of proteins.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Fang EF,Wong JH,Lin P,Ng TB

doi

10.1016/j.febslet.2010.08.041

subject

Has Abstract

pub_date

2010-09-24 00:00:00

pages

4089-96

issue

18

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(10)00703-9

journal_volume

584

pub_type

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