Relationship between dicotyledone-amaranth, quinoa, fagopyrum, soybean and monocots- sorghum and rice based on protein analyses and their use as substitution of each other

Angiotensin I-converting enzyme-inhibitory peptide fractions from albumin 1 and globulin as obtained of amaranth grain

“…In addition, the electrophoretic profiles of albumin 1 and globulin, (Fig. 1) were very similar to those reported by Gorinstein et al (2005). Because 5% of Na 2 SO 4 extracted less non-protein nitrogen than 29.3% NaCl, the former solution was chosen to extract proteins to prepare peptide fractions in this work.…”

Comparison between isoelectric precipitation and ultrafiltration processes to obtain Amaranth mantegazzianus protein concentrates at pilot plant scale

“…Gamel et al (2005) found polypeptides in the range of 14-94 kDa in the electrophoretic profiles of proteins from A. cruentus and A. caudatus, with major bands of 78, 55, 43, 36, 27 and 17 kDa. The low resolution of bands in the region of low molecular weight (<20 kDa) is consistent with Gorinstein et al (2005), which report that SDS-PAGE profiles in this region are weak and not discernible for proteins of different varieties of amaranth.…”

“…This profile is similar to those reported in the literature for other amaranth varieties. Gorinstein et al (2005) found 28-39 bands in the range of 14-97 kDa in the electrophoretic profiles of A. hybridum, A. cruentus and A. hypochondriacus. Gamel et al (2005) found polypeptides in the range of 14-94 kDa in the electrophoretic profiles of proteins from A. cruentus and A. caudatus, with major bands of 78, 55, 43, 36, 27 and 17 kDa.…”

Characterisation of the Amaranth Genetic Resources in the Czech Gene Bank

“…The division of the grain amaranth glutelins into three major groups reported also Gorinstein et al (2004) (Drzewiecki, 2001;Marcone, 2002;Gorinstein et al, 2005), but its position was determined differently: as 55 kDa (Marcone, 2002) or 52 kDa (Drzewiecki, 2001) or in the case of protein fractions as 55 kDa, too (Thanapornpoonpong et al, 2008). The characteristic presence of the band 58 kDa in A. cruentus spectra and of the band 54 kDa in A. hypochondriacus spectra was confirmed by the results of Thanapornpoonpong et al (2008).…”

“…The bulked samples of 10 seeds extracted in 100 μl to be the most suitable tools, because of their clear expression of protein patterns and moreover they can be used when samples with higher number of seeds are not available. This selected approach differed from methodology selected by Drzewiecki (2001) who used 50 μl or by Gorinstein et al (2005) who used 62.5 μl of extraction solution for 10 seeds bulked samples. The need for using more extraction solution in our study might be to consequence of higher protein extraction as a result of the proper seed crushing performed in our study which was not mentioned in the methodology description of other authors (Drzewiecki, 2001;Gorinstein et al, 2005).…”