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Isolation of a napin‐like polypeptide with potent translation‐inhibitory activity from chinese cabbage ( Brassica parachinensis cv green‐stalked) seeds
Author(s) -
Ngai Patrick H. K.,
Ng T. B.
Publication year - 2003
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.460
Subject(s) - fast protein liquid chromatography , brassica , size exclusion chromatography , chemistry , chromatography , biochemistry , affinity chromatography , ion chromatography , bioorganic chemistry , high performance liquid chromatography , biology , botany , enzyme
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 IC 50 of 6.2 n M . 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.