A new distinct group of 2 S albumins from rapeseed. Amino acid sequence of two low molecular weight napins.
Two napins (nIa and nIb), isolated from Brassica napus (rapeseed) seeds, have been sequenced. The two proteins show the common structural pattern of the 2 S albumins, since they are composed of two disulfide-linked chains of different size, yet they exhibit an atypical low molecular weight (12.5 kDa vs. 14.5 kDa of the major napins). High sequence similarity has been found between these 2 proteins, but only 54% similarity can be estimated from their comparison with the 14.5 kDa major napins. Thus, nIa and nIb are considered representatives of a new distinct group of rapeseed napins since all the previously known napins exhibit 95% sequence similarity. Unexpectedly, the similarity increases when compared with the 2 S proteins from other species.
Monsalve
R I
RI
Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad Complutense, Madrid, Spain.
Lopez-Otin
C
C
Villalba
M
M
Rodríguez
R
R
D055516:2S Albumins, Plant; D000418:Albumins / Q000737:chemistry* / Q000302:isolation & purification; D000595:Amino Acid Sequence; D001937:Brassica / Q000737:chemistry* / Q000235:genetics; D010450:Endopeptidases; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D010944:Plants / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid
D055516:2S Albumins, Plant; D000418:Albumins; D010446:Peptide Fragments; D010940:Plant Proteins; C050363:napin protein, Brassica napus; D010450:Endopeptidases