Identification of cultivars of Stylosanthes capitata Vog. by polyacrylamide gel electrophoresis of seed proteins

Euphytica ◽  
1988 ◽  
Vol 37 (2) ◽  
pp. 117-119
Author(s):  
A. Hussain ◽  
H. Ramirez ◽  
W. Bushuk ◽  
W. M. Roca
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Polyacrylamide Gel

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

DISCRIMINATION OF CULTIVARS OF LENTIL (Lens culinaris Medic.) BY ELECTROPHORESIS OF SEED PROTEINS

1989 ◽  
Vol 69 (1) ◽  
pp. 243-246 ◽  
Author(s):  
A. HUSSAIN ◽  
W. BUSHUK ◽  
K. W. CLARK
Keyword(s):  
Gel Electrophoresis ◽  
Lens Culinaris ◽  
Seed Protein ◽  
Cultivar Identification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Polyacrylamide Gel

Discrimination of lentil cultivars was achieved by analysis of seed protein by two types of polyacrylamide gel electrophoresis. Cultivars of lentil were discriminated by the presence or absence of diagnostic bands. Electrophoregrams of six seed lots of the cultivar Eston were identical and unaffected by growing conditions.Key words: Lens culinaris Medic, seed proteins, polyacrylamide gel electrophoresis, cultivar identification

IDENTIFICATION OF CICER MILKVETCH CULTIVARS USING SDS-POLYACRYLAMIDE GEL ELECTROPHORESIS

1983 ◽  
Vol 63 (4) ◽  
pp. 1087-1090 ◽  
Author(s):  
ROBERT K. EVANS ◽  
ROLLIN H. ABERNETHY
Keyword(s):  
Banding Pattern ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Polyacrylamide Gel ◽  
Forage Legumes ◽  
Electrophoretic Method ◽  
Stand Establishment ◽  
Astragalus Cicer ◽  
Varietal Purity

With the release of Monarch cicer milkvetch (Astragalus cicer L.), which has greatly facilitated stand establishment when compared to older cultivars, the desirability of a method for identifying seed of cultivars was recognized. An SDS-polyacrylamide gel electrophoretic method was developed to differentiate cicer milkvetch cultivars. Densitometric scanning of the resultant polypeptide banding pattern on the polyacrylamide gel provided identification of seed lots of the cultivars Oxley, Lutana and Monarch produced in several different years and locations.Key words: Astragalus cicer L., forage legumes, seed proteins, varietal purity

scholarly journals Polyacrylamide gel electrophoresis of soybean seed proteins

2015 ◽  
Vol 47 (4) ◽  
pp. 371-378 ◽  
Author(s):  
W. Lassocińsk ◽  
J. S. Knypl
Keyword(s):  
Glycine Max ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Soybean Seed ◽  
Seed Proteins ◽  
Soluble Proteins ◽  
Polyacrylamide Gel ◽  
Major Protein ◽  
Molecular Weights ◽  
Minor Protein

Four major and 14 minor protein bands were detected when total salt soluble proteins of soybean (Glycine max cultivar Warszawska) seed were subjected to polyacrylamide gel electrophoresis under nondissociating conditions, and 16 protein bands were detected under dissociating conditions. Molecular weights of three major protein fractions in PAGE SDS were determined for around 18 500, 36 000 and 80 000 daltons.

A COMPARATIVE STUDY OF SEED PROTEINS OF ALLOPOLYPLOIDS OF GOSSYPIUM BY GEL ELECTROPHORESIS

1971 ◽  
Vol 13 (1) ◽  
pp. 155-158 ◽  
Author(s):  
J. P. Cherry ◽  
F. R. H. Katterman ◽  
J. E. Endrizzi
Keyword(s):  
Comparative Study ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gene Mutations ◽  
Seed Proteins ◽  
Polyacrylamide Gel ◽  
Synthetic Mixture ◽  
Banding Patterns ◽  
Regulatory Systems ◽  
Species Specific

Polyacrylamide gel electrophoresis of seed proteins from recently synthesized F1 triploid and colchicine-induced hexaploid plants showed the additive banding patterns of their parents (G. hirsutum × G. sturtianum) when compared to the synthetic mixture of the latter. Gene mutations, diploidization and species specific regulatory systems are discussed as possible evolutionary processes for the protein banding differences in the allopolyploids of the genus Gossypium.

Ultrastructural localization of specific nucleoprotein fractions

1978 ◽  
Vol 36 (2) ◽  
pp. 204-205
Author(s):  
G. L. Brown
Keyword(s):  
Gel Electrophoresis ◽  
Mouse Liver ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ultrastructural Localization ◽  
Polyacrylamide Gel ◽  
Acid Extraction ◽  
Acid Solutions ◽  
Low Salt ◽  
Liver Nuclei ◽  
Phosphate Groups

Bismuth (Bi) stains nucleoproteins (NPs) by interacting with available amino and primary phosphate groups. These two staining mechanisms are distinguishable by glutaraldehyde crosslinking (Fig. 1,2).Isolated mouse liver nuclei, extracted with salt and acid solutions, fixed in either formaldehyde (form.) or gl utaraldehyde (glut.) and stained with Bi, were viewed to determine the effect of the extractions on Bi stainina. Solubilized NPs were analyzed by SDS-polyacrylamide gel electrophoresis.Extraction with 0.14 M salt does not change the Bi staining characteristics (Fig. 3). 0.34 M salt reduces nucleolar (Nu) staining but has no effect on interchromatinic (IC) staining (Fig. 4). Proteins responsible for Nu and glut.- insensitive IC staining are removed when nuclei are extracted with 0.6 M salt (Fig. 5, 6). Low salt and acid extraction prevents Bi-Nu staining but has no effect on IC staining (Fig. 7). When nuclei are extracted with 0.6 M salt followed by low salt and acid, all Bi-staining components are removed (Fig. 8).

Platelet Microtubule Subunit Proteins

1979 ◽  
Vol 42 (05) ◽  
pp. 1630-1633 ◽  
Author(s):  
A G Castle ◽  
N Crawford
Keyword(s):  
Epithelial Cells ◽  
Gel Electrophoresis ◽  
Blood Platelets ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Lens Epithelial Cells ◽  
Molecular Weights ◽  
Kinetics Of ◽  
Microtubular Structures

SummaryBlood platelets contain microtubule proteins (tubulin and HMWs) which can be polymerised “in vitro” to form structures which resemble the microtubules seen in the intact platelet. Platelet tubulin is composed of two non-identical subunits a and p tubulin which have molecular weights around 55,000 but can be resolved in alkaline SDS-polyacrylamide gel electrophoresis. These subunits associate as dimers with sedimentation coefficients of about 5.7 S although it is not known whether the dimer protein is a homo- or hetero-dimer. The dimer tubulin binds the anti-mitotic drug colchicine and the kinetics of this binding are similar to those reported for neurotubulins. Platelet microtubules also contain two HMW proteins which appear to be essential and integral components of the fully assembled microtubule. These proteins have molecular weights greater than 200,000 daltons. Fluorescent labelled antibodies to platelet and brain tubulins stain long filamentous microtubular structures in bovine lens epithelial cells and this pattern of staining is prevented by exposing the cells to conditions known to cause depolymerisation of cell microtubules.

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