Characterization of the major proteins of tubers of yam bean (Pachyrhizus ahipa).
Tubers of six accessions of ahipa (Pachyrhizus ahipa) contained between 0.77 and 1.34% nitrogen on a dry weight basis. This corresponds to 4.8 to 8.4% crude protein based on a nitrogen to protein conversion factor of 6.25; but detailed analysis of AC230 showed that although 93% of the total N was extracted with buffer containing 1.0 M NaCl, about a third of this was lost on dialysis. It was calculated, therefore, that salt-soluble proteins comprise about 60% of the total tuber nitrogen, with low-molecular-mass nitrogenous components comprising a further 30%. Electophoretic analysis of the salt-soluble proteins showed similar patterns of components in the six accessions, with none being present in amounts sufficiently high to suggest a role as storage proteins. Furthermore, light microscopy failed to show significant deposits of protein within the tuber cells. Five "major" protein bands, which together accounted for about 19% of the total salt-soluble protein fraction were purified and subjected to N-terminal amino acid sequencing. Comparison of these with sequences in protein databases revealed similarities to alpha-amylases, chitinases and chitin binding proteins, cysteine proteinases (including major components from P. erosus tubers), a tuberization-specific protein from potato, and proteins induced in soybean and pea by stress or the plant hormone abscisic acid, respectively. It was concluded that the primary roles of these proteins are probably in aspects of tuber metabolism and development and/or conferring protection to pests and pathogens, and that true storage proteins are not present. The absence of storage proteins is consistent with the biological role of the tubers as storage organs for carbohydrates (cf cassava tuberous roots) rather than as propagules (cf yam and potato tubers).
Forsyth
Jane L
JL
IACR Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, Long Ashton, Bristol BS41 9AF, U.K.
Shewry
Peter R
PR
D000595:Amino Acid Sequence; D015153:Blotting, Western; D002688:Chitinases / Q000032:analysis; D003546:Cysteine Endopeptidases / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D005612:Freeze Drying; D008970:Molecular Weight; D009584:Nitrogen / Q000032:analysis; D029905:Pachyrhizus / Q000737:chemistry*; D010940:Plant Proteins / Q000032:analysis* / Q000737:chemistry; D018514:Plant Structures / Q000737:chemistry*; D012639:Seeds / Q000737:chemistry; D000516:alpha-Amylases / Q000032:analysis
D010940:Plant Proteins; D000516:alpha-Amylases; D002688:Chitinases; D003546:Cysteine Endopeptidases; D009584:Nitrogen