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A ribonuclease from Chinese ginseng (Panax ginseng) flowers.

Authors :
Wang HX
Ng TB
Source :
Protein expression and purification [Protein Expr Purif] 2004 Feb; Vol. 33 (2), pp. 195-9.
Publication Year :
2004

Abstract

A ribonuclease, with a molecular mass of 23kDa, and much higher activity toward poly(U) than poly(C) and only negligible activity toward poly(A) and poly(G), was isolated from the aqueous extract of Chinese ginseng (Panax ginseng) flowers. The ribonuclease was unadsorbed on diethylaminoethyl-cellulose and adsorbed on Affi-gel blue gel and carboxymethyl-cellulose. High activity of the ribonuclease was maintained at pH 6-7. On either side of this pH range, there was a precipitous drop in enzyme activity. The activity of the enzyme peaked at 50 degrees C and fell to about 20% of the maximal activity when the temperature was lowered to 20 degrees C or raised to 80 degrees C. The characteristics of this ribonuclease were different from those of ribonuclease previously purified from ginseng roots.

Details

Language :
English
ISSN :
1046-5928
Volume :
33
Issue :
2
Database :
MEDLINE
Journal :
Protein expression and purification
Publication Type :
Academic Journal
Accession number :
14711506
Full Text :
https://doi.org/10.1016/j.pep.2003.09.002