Isolation of a napin-like polypeptide with potent translation-inhibitory activity from chinese cabbage (Brassica parachinensis cv green-stalked) seeds

A heterodimeric napin‐like polypeptide was isolated from Brassica parachinensis seeds with a procedure involving ion exchange chromatography on DEAE‐cellulose, affinity chromatography on Affi‐gel blue gel, FPLC‐ion exchange chromatography on Mono S and FPLC‐gel filtration on Superdex 75. The N‐termi...

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Veröffentlicht in:	Journal of peptide science 2003-07, Vol.9 (7), p.442-449
Hauptverfasser:	Ngai, Patrick H. K., Ng, T. B.
Format:	Artikel
Sprache:	eng
Schlagworte:	2S Albumins, Plant Amino Acid Sequence Animals Brassica Brassica - chemistry Brassica parachinensis cabbage Cell-Free System Chromatography, Affinity Chromatography, Gel Electrophoresis, Polyacrylamide Gel Molecular Sequence Data napin Plant Proteins - isolation & purification Plant Proteins - pharmacology Protein Biosynthesis - drug effects seeds Seeds - chemistry Sequence Analysis, Protein translation-inhibitory activity
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Zusammenfassung:	A heterodimeric napin‐like polypeptide was isolated from Brassica parachinensis seeds with a procedure involving ion exchange chromatography on DEAE‐cellulose, affinity chromatography on Affi‐gel blue gel, FPLC‐ion exchange chromatography on Mono S and FPLC‐gel filtration on Superdex 75. The N‐terminal sequence of the 5 kDa subunit of the polypeptide (PAGPFRIPKKRKKEE) showed high homology with other 2S storage proteins like napins and albumins. The polypeptide potently inhibited translation in a cell free system with an IC50 of 6.2 nM. The translation‐inhibiting activity of the polypeptide was relatively stable in the pH range 6–11 and in the temperature range 10–50°C. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.
ISSN:	1075-2617 1099-1387
DOI:	10.1002/psc.460