2002Egyptian Journal of Agricultural Sciences /Egyptian Journal of Agricultural SciencesOpen access

COMPARATIVE STUDY ON STORAGE PROTEINS OF OLIVE SEEDS Olea europea AND OLEACEAE

M. K. Sousow

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Abstract

Among the slorage proteins in olive seeds' an abundant gllcoprolein \ith MW of 49.2 kDa (GP50) is oonsidered a homopolymer which is dissociated in the prcsence of detergent SDS in non-reducitlg conditions and constitutes aboui 109i' of these proteins (Sousot\', 2001).]n rhe presenl study, this protei was purified by preparative electrophoresis after dcgllrosylation of oligosaccharides moieties b] a chemical mcthod in order to prepare an immunsera-'fhe carboh)drate moi€ty of CP50 *as analYssd lt contained galaclose, x)losc, mannosc and N-aceql_glucosamine residues in a ralio of2.5: 2il:2.The preparation ofanlibodies specilic for GP50 pennited the immun,,(hcmlcrl (xraclcri/dllon Jl IIir lr.rreinThere \\as a strong homologl in the polypeptides composition of srorage proteins from seeds of diilcrent ol;vc cultivars of (r1e.r e r.rPea.Howcve!, antibodies specific for GP50 were immonodetected polypeptides specific for spanish va cties' Proteins of similar molccular weights and antibodies related lo CP50 \\ere immunodctecled in al1 Oleaceae sceds examined' l

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Among the slorage proteins in olive seeds' an abundant gllcoprolein \ith MW of 49.2 kDa (GP50) is oonsidered a homopolymer which is dissociated in the prcsence of detergent SDS in non-reducitlg conditions and constitutes aboui 109i' of these proteins (Sousot\', 2001).]n rhe presenl study, this protei was purified by preparative electrophoresis after dcgllrosylation of oligosaccharides moieties b] a chemical mcthod in order to prepare an immunsera-'fhe carboh)drate moi€ty of CP50 *as analYssd lt contained galaclose, x)losc, mannosc and N-aceql_glucosamine residues in a ralio of2.5: 2il:2.The preparation ofanlibodies specilic for GP50 pennited the immun,,(hcmlcrl (xraclcri/dllon Jl IIir lr.rreinThere \\as a strong homologl in the polypeptides composition of srorage proteins from seeds of diilcrent ol;vc cultivars of (r1e.r e r.rPea.Howcve!, antibodies specific for GP50 were immonodetected polypeptides specific for spanish va cties' Proteins of similar molccular weights and antibodies related lo CP50 \\ere immunodctecled in al1 Oleaceae sceds examined' l

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Available abstract

Among the slorage proteins in olive seeds' an abundant gllcoprolein \ith MW of 49.2 kDa (GP50) is oonsidered a homopolymer which is dissociated in the prcsence of detergent SDS in non-reducitlg conditions and constitutes aboui 109i' of these proteins (Sousot\', 2001).]n rhe presenl study, this protei was purified by preparative electrophoresis after dcgllrosylation of oligosaccharides moieties b] a chemical mcthod in order to prepare an immunsera-'fhe carboh)drate moi€ty of CP50 *as analYssd lt contained galaclose, x)losc, mannosc and N-aceql_glucosamine residues in a ralio of2.5: 2il:2.The preparation ofanlibodies specilic for GP50 pennited the immun,,(hcmlcrl (xraclcri/dllon Jl IIir lr.rreinThere \\as a strong homologl in the polypeptides composition of srorage proteins from seeds of diilcrent ol;vc cultivars of (r1e.r e r.rPea.Howcve!, antibodies specific for GP50 were immonodetected polypeptides specific for spanish va cties' Proteins of similar molccular weights and antibodies related lo CP50 \\ere immunodctecled in al1 Oleaceae sceds examined' l

Key concepts: Olea, Oleaceae, Botany, Horticulture, Biology

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