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.

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

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.

scholarly journals Studies on Platelet Glycoproteins by Surface Labeling and SDS Polyacrylamide Gel Electrophoresis

1977 ◽  
Author(s):  
I. Hagen ◽  
N.O. Solum ◽  
M. Peterka
Keyword(s):  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Conformational State ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Metabolic Inhibitors ◽  
Conventional System ◽  
Platelet Surface ◽  
Release Reaction

Platelet surface (glyco)proteins, and alterations in these in connection with the thrombin-induced release reaction has been studied. Platelets were labeled by lactoperoxidase-catalyzed iodination, and examined by SDS gel electrophoresis in two different gel systems, one conventional(J. Biol. Chem.1969 244 4406), and the other containing urea and EDTA in the gels. In the conventional system the bulk of radioactivity coincided with a PAS band (GP III) of MW about 100, 000. In the other system, the main radioactive peak appeared in the GP II area (MW 120,000), and a shift in the PAS stain intensity from GP III to GP II was seen. Thrombasthenic platelets showed only traces of the GP II band in both systems. The bulk of radioactivity was associated with the surface glycopolypeptide GPS, which is present, but not labeled in normal platelets. In thrombin-released platelets, GPS in its unreduced state has an altered electrophoretic mobility compared to control platelets and platelets which have been incubated with metabolic inhibitors to prevent secretion. The findings indicate that the GP III band consists of two different polypeptides, one of which appears in the GP II area in gels containing urea and EDTA. Further, that thrombasthenic platelet membrane exists in a conformational state different from that of normal platelets. And finally, GPS is in some way involved in, or influenced by, the thrombin-induced release reaction.

POLAR BEAR MILK: III. GEL-ELECTROPHORETIC STUDIES OF PROTEIN FRACTIONS ISOLATED FROM POLAR BEAR MILK AND HUMAN MILK

1967 ◽  
Vol 45 (6) ◽  
pp. 1205-1210 ◽  
Author(s):  
B. E. Baker ◽  
V. B. Hatcher ◽  
C. R. Harington
Keyword(s):  
Sialic Acid ◽  
Acid Content ◽  
Polar Bear ◽  
Whey Proteins ◽  
Electrophoretic Analysis ◽  
Polyacrylamide Gel ◽  
Sialic Acid Content ◽  
Electrophoretic Patterns ◽  
Centrifuge Tube ◽  
Starch Gel

Polar bear milk was stored in the frozen state for 2 months. It was then thawed and subjected to low-speed centrifugation. The material (D) which deposited at the bottom of the centrifuge tube and also the casein and whey proteins isolated from the supernate were analyzed by polyacrylamide-gel (without urea) electrophoresis. The precipitate (D) and the casein gave closely similar electrophoretic patterns. However, the precipitate (D) contained less than 20% of the carbohydrate (hexose, hexosamine, sialic acid) content of the casein. Polar bear casein and bovine casein gave similar electropherograms when subjected to polyacrylamide-gel (7 M urea) electrophoretic analysis. Human casein gave eight distinct bands, four of which had higher mobilities than did bovine αs-casein. Starch-gel (2-mercaptoethanol added) electrophoretic analysis indicated that polar bear casein and human casein produced 8 and 13 electrophoretic components respectively.

scholarly journals Identification of Hiochi Bacteria by Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoretic Patterns of Whole Cell Proteins.

1991 ◽  
Vol 55 (10) ◽  
pp. 2455-2460 ◽  
Author(s):  
Jinshichiro NAKAMURA ◽  
Kenji Doi ◽  
Yuko HIGASHIDA ◽  
Masaaki HAMACHI ◽  
Takemitsu HONMA
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Whole Cell ◽  
Electrophoretic Patterns ◽  
Dodecyl Sulfate

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
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