Premium
Biochemical characterization of the RNA‐hydrolytic activity of a pumpkin 2S albumin
Author(s) -
Fang Evandro Fei,
Wong Jack Ho,
Lin Peng,
Ng Tzi Bun
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.08.041
Subject(s) - rnase p , ribonuclease , rna , cucurbita , biochemistry , hydrolysis , pumpkin seed , albumin , chemistry , yeast , cucurbita pepo , rnase h , enzyme , microbiology and biotechnology , biology , food science , botany , gene
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.