Amaranth seed proteins: Effect of defatting on extraction yield and on electrophoretic patterns

1995 ◽  
Vol 47 (1) ◽  
pp. 49-53 ◽  
Author(s):  
N. E. Leyva-Lopez ◽  
N. Vasco ◽  
A. P. Barba de la Rosa ◽  
O. Paredes-Lopez
Keyword(s):  
Seed Proteins ◽  
Extraction Yield ◽  
Electrophoretic Patterns ◽  
Amaranth Seed

IDENTIFICATION OF CULTIVARS OF FORAGE LEGUME (Desmodium ovalifolium GUILL ET PERR.) BY THEIR ELECTROPHORETIC PATTERNS

1987 ◽  
Vol 67 (3) ◽  
pp. 713-717 ◽  
Author(s):  
A. HUSSAIN ◽  
W. BUSHUK ◽  
H. RAMIREZ ◽  
W. ROCA
Keyword(s):  
Gel Electrophoresis ◽  
Cultivar Identification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Polyacrylamide Gel ◽  
Forage Legume ◽  
Desmodium Ovalifolium ◽  
Electrophoretic Patterns ◽  
Electrophoretic Procedure

An electrophoretic procedure was developed for discriminating cultivars of Desmodium ovalifolium on the basis of patterns of partially purified seed proteins. Electrophoresis was done on uniform 15% polycrylamide gels in basic (8.9) pH. The method produced satisfactory discrimination of eight cultivars used in its initial evaluation.Key words: Forage legume, Desmodium ovalifolium Guill et Perr., cultivar identification, polyacrylamide gel electrophoresis

INFLUENCE OF SOURCE OF WHEAT CYTOPLASM ON THE NATURE OF PROTEINS IN HEXAPLOID TRITICALE

1974 ◽  
Vol 16 (3) ◽  
pp. 529-537 ◽  
Author(s):  
S. L. K. Hsam ◽  
E. N. Larter
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Proteins ◽  
Triticum Aestivum L ◽  
The Other ◽  
Hexaploid Triticale ◽  
Electrophoretic Patterns ◽  
High Molecular Weight Proteins

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to study seed proteins in 4 pairs of reciprocal F1 isogenic hybrids of hexaploid triticales differing only in their source of cytoplasm. One member of each reciprocal pair possessed the cytoplasm of hexaploid (6x) wheat (Triticum aestivum L. em. Thell), the other, the cytoplasm from tetraploid (4x) wheat (T. turgidum L). Qualitative as well as quantitative differences were observed in the electrophoretic patterns of the albumins and globulins. High molecular weight proteins (> 34,000 daltons) were synthesized in triticale with 6x wheat cytoplasm in greater quantity than in triticale with 4x wheat cytoplasm. Differences in the patterns of gliadin and reduced glutenin of the reciprocal triticale populations were quantitative. The relevance of these findings to seed development in triticales is discussed.

scholarly journals Seed protein variability in safflower

2002 ◽  
pp. 29-34
Author(s):  
Dragana Obreht ◽  
Ljiljana Vapa ◽  
Sándor Kis ◽  
Mária-Hajos Takács ◽  
Éva-Bányai Stefánovics ◽  
...  
Keyword(s):  
Protein Content ◽  
Seed Protein ◽  
Seed Proteins ◽  
Carthamus Tinctorius ◽  
Seed Protein Content ◽  
Electrophoretic Patterns ◽  
Sds Page ◽  
The Usa ◽  
Molecular Masses ◽  
Total Seed

Total seed proteins in two safflower species (Carthamus tinctorius L. and C. lanatus L) have been separated by the SDS-PAGE method. Their molecular masses ranged from 120 to 20 kDa. All C. tinctorius genotypes under study exhibited identical electrophoretic patterns which differed from the pattern exhibited by the wild species C. lanatus in the number and position of protein bands. Differences in protein profiles occurred in regions around 60 kDa, from 43 to 36 kDa and around 30 kDa. Statistically significant differences in seed protein content were found among safflower genotypes from different countries as well as among genotypes from the same country but from different sites. The highest seed protein content was found in a genotype originating from the USA.

scholarly journals Sequence Identification of Bioactive Peptides from Amaranth Seed Proteins (Amaranthus hypochondriacus spp.)

Molecules ◽  
2019 ◽  
Vol 24 (17) ◽  
pp. 3033 ◽  
Author(s):  
Alexis Ayala-Niño ◽  
Gabriela Mariana Rodríguez-Serrano ◽  
Luis Guillermo González-Olivares ◽  
Elizabeth Contreras-López ◽  
Patricia Regal-López ◽  
...  
Keyword(s):  
Biological Activity ◽  
Bioactive Peptides ◽  
Continuous Process ◽  
Seed Proteins ◽  
Thrombin Inhibitors ◽  
Amaranthus Hypochondriacus ◽  
Potential Source ◽  
Sequence Identification ◽  
Amaranth Seed ◽  
Bioactive Potential

Amaranthus hypochondriacus spp. is a commonly grown cereal in Latin America, known for its high protein content. The objective of this study was to separate and identify bioactive peptides found in amaranth seeds through enzymatically-assisted hydrolysis using alcalase and flavourzyme. Hydrolysis was carried out for each enzyme separately and compared to two-step continuous process where both enzymes were combined. The biological activity of the resulting three hydrolysates was analyzed, finding, in general, higher bioactive potential of the hydrolysate obtained in a continuous process (combined enzymes). Its fractions were separated by RP-HPLC, and their bioactivity was analyzed. In particular, two fractions showed the highest biological activity as ACE inhibitors with IC50 at 0.158 and 0.134, thrombin inhibitors with IC50 of 167 and 155, and antioxidants in ABTS assay with SC50 at 1.375 and 0.992 mg/L, respectively. Further sequence analysis of the bioactive peptides was carried out using MALDI-TOF, which identified amino acid chains that have not been reported as bioactive so far. Bibliographic survey allowed identification of similarities between peptides reported in amaranth and other proteins. In conclusion, amaranth proteins are a potential source of peptides with multifunctional activity.

scholarly journals Electrophoretic patterns of reserve seed proteins with reference to the taxonomic comparison of bean cultivars

2013 ◽  
Vol 39 (2) ◽  
pp. 201-206
Author(s):  
Janusz Czapski ◽  
Ryszard Kkosson
Keyword(s):  
Phaseolus Vulgaris ◽  
Electrophoretic Mobility ◽  
Seed Proteins ◽  
Similarity Coefficient ◽  
Polyacrylamide Gel ◽  
Qualitative And Quantitative ◽  
Electrophoretic Patterns ◽  
Seed Albumins ◽  
Seed Globulins

The seed albumins and seed globulins of five Polish cultivars of <i>Phaseolus vulgaris</i> and one cultivar of <i>Phaseolus multiflorus</i> were electrophoretically separated in polyacrylamide gel using the disc-technique of Orstein and Davis. To compare any two cultivars, the percentage of similarity coefficient (<i>S</i>) was calculated based on the Rp values of protein bands. It was found that the electrophoretic mobility of the bean globulins is in general lower than albumins. Cultivar 'Piękny Jaś', belonging to <i>Phaseolus multiflorus</i> species showed large qualitative and quantitative differences in the albumin and globulin patterns as compared to other cultivars belonging to <i>Phaseolus vulgaris</i> species.

Fractionation procedures, electrophoretic characterization, and amino acid composition of amaranth seed proteins

1992 ◽  
Vol 40 (6) ◽  
pp. 931-936 ◽  
Author(s):  
Ana P. Barba de la Rosa ◽  
Jacques. Gueguen ◽  
Octavio. Paredes-Lopez ◽  
Gerard. Viroben
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Seed Proteins ◽  
Amaranth Seed

FIELD PEA CULTTVAR IDENTIFICATION BY ELECTROPHORETIC PATTERNS OF COTYLEDON PROTEINS

1988 ◽  
Vol 68 (4) ◽  
pp. 1143-1147 ◽  
Author(s):  
A. HUSSAIN ◽  
W. BUSHUK ◽  
S. T. ALI-KHAN
Keyword(s):  
Acetic Acid ◽  
Pisum Sativum ◽  
Cultivar Identification ◽  
Seed Proteins ◽  
Field Pea ◽  
Polyacrylamide Gels ◽  
Electrophoretic Patterns ◽  
Pisum Sativum L ◽  
Page Electrophoresis

A procedure was developed for discrimination and identification of cultivars of field pea (Pisum sativum L.) on the basis of the electrophoretic patterns of the acetic acid soluble seed proteins. The electrophoresis is done on 7% polyacrylamide gels at pH 3.1 in aluminum lactate buffer.Key words: Pea, Pisum sativum L., cultivar identification, lactate PAGE, electrophoresis

scholarly journals Affinity Grouping of Lentil Accessions through Comparative Electrophoresis of Seed Proteins

HortScience ◽  
1997 ◽  
Vol 32 (3) ◽  
pp. 452D-452
Author(s):  
S. Echeverrigaray ◽  
A.C. Oliveira ◽  
M.T.V. Carvalho ◽  
E. Derbyshire
Keyword(s):  
Biochemical Analysis ◽  
Genetic Relationships ◽  
Seed Proteins ◽  
Breeding Programs ◽  
Qualitative And Quantitative ◽  
Bank Management ◽  
Electrophoretic Patterns ◽  
Affinity Groups ◽  
The Individual

The comparison of the electrophoretic patterns of seed polypeptides and basic proteins of 40 lentil germplasm accessions revealed a wide qualitative and quantitative variation that allowed the individual characterization of all the genotypes. The statistical analysis of the variation and the clustering of the samples by multivariate methods allowed the construction of five affinity groups that were consistent with the origin and genetic relationships among the accessions. These results indicate the reliability of this simple and inexpensive biochemical analysis in lentil germplasm bank management, cultivar identification and monitoring, and the construction of affinity groups that can help breeding programs.

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