Comparative study of the protein patterns of some rapeseed (Brassica napus L.) varieties by means of polyacrylamide gel electrophoresis and high‐performance liquid chromatography

Abstract

SummarySeven rapeseed varieties were characterized by investigation of the patterns of buffer soluble proteins using polyacrylamide gel electrophoresis and high-performance liquid chromatography (size-exclusion and cation-exchange chromatography). Most pronounced differences were found in proteins not belonging to 12 S and 2 S storage proteins having presumably metabolic functions. Quantitative variations dominate within the low molecular mass 2 S storage proteins. ZusammenfassungVergleichende Untersuchung der Proteinmuster einiger Rapsvarietaten ( B . nupus L.) mit Hilfe von Polyacrylamid-Gelektrophorese und Hochleistungs-Flussigchromatographie 7 Rapsvarietaten wurden durch Untersuchung der pufferloslichen Proteinfraktionen mittels Polyacrylamid-Gelelektrophorese und Hochleistungs-Flussigchromatographie (Gelpermeations-und Kationenaustauschchromatographie) charakterisiert. Die deutlichsten Unterschiede zwischen den Varietaten traten in Proteinfraktionen auf, die weder zu den 12-S-noch zu den 2-S-Speicherproteinen gehoren, sondern moglichenveise biologisch aktive Fraktionen darstellen. Charakteristische quantitative Unterschiede wurden in der 2-S-Speicherprotein-Fraktion festgestellt.

Allergens and Toxins from Oleaginous Plants: Problems and Solutions

“…The large chain includes two additional intrachain disulphide bonds, which reinforce the stability of the proteins (Byczynska & Barciszewski, 1999;Monsalve & Rodriguez, 1990). Napins are characterised by their strong basicity (isoelectric point, pI ~ 11) mainly due to a high amidation of amino acids (Raab et al, 1992). Napins are polymorphic proteins due to their origin from multigene families.…”

“…They can be classified into three classes according to molecular weight 12.5, 14.5 and 15 kDa (Monsalve & Rodrigues, 1990). Mature napins exhibit molecular weights between 12,500 and 14,500 Da (Raab et al, 1992). They are encoded by a multigenic family, initially synthesized as a precursor which is proteolytically cleaved to generate mature napin chains.…”

“…After oil extraction, a meal is obtained containing most of the proteins (30-40%) (Boucher et al, 2007;Pantoja-Uceda et al, 2004). Rapeseed protein meal contains two predominant classes of seed storage proteins: 12S globulin (cruciferin) which represents 25-65% of its protein content (Raab et al, 1992) and 2S albumin (napin). Napins belong to the 2S albumin class of proteins and hence are water soluble, stable at high temperature (up to 88±C) (Krzyzaniak, et al, 1998) and represent 15-45% of the total rape seed protein content depending on the variety (Raab et al, 1992).…”

“…Rapeseed protein meal contains two predominant classes of seed storage proteins: 12S globulin (cruciferin) which represents 25-65% of its protein content (Raab et al, 1992) and 2S albumin (napin). Napins belong to the 2S albumin class of proteins and hence are water soluble, stable at high temperature (up to 88±C) (Krzyzaniak, et al, 1998) and represent 15-45% of the total rape seed protein content depending on the variety (Raab et al, 1992). These proteins belong to the albumin storage proteins; in the seeds of recent varieties, they are present in lower quantities than cruciferins.…”

Separation of low molecular weight rapeseed proteins by RP-HPLC-DAD - a short report

“…According to various authors, their molecular mass ranges from 12 000 to 18 000 (AMA-ROWICZ et al 1993). For the separation of low molecular weight rapeseed proteins, HPLC method with ionexchange columns Shodex IEC-CM 825 (RAAB et al 1992) and Mono Q (AMAROWICZ et al 1993) as well capillary electrophoresis (MEKB with SDS as the surfactant) (AMAROWICZ et al 2003a) were used.…”