Identification of cultivars of pasture legumes (Centrosema macrocarpum, C. pubescens and C. sp.n.) by acid polyacrylamide gel electrophoresis of cotyledons storage proteins

Euphytica ◽  
1988 ◽  
Vol 39 (2) ◽  
pp. 105-107 ◽  
Author(s):  
A. Hussain ◽  
H. Ramirez ◽  
W. M. Roca ◽  
W. Bushuk
Keyword(s):  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Pasture Legumes

Diversity of seed storage proteins in common wheat (Triticum aestivum L.)

2011 ◽  
Vol 9 (2) ◽  
pp. 256-259
Author(s):  
Zuzana Šramková ◽  
Edita Gregová ◽  
Svetlana Šliková ◽  
Ernest Šturdík
Keyword(s):  
Triticum Aestivum ◽  
Common Wheat ◽  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Triticum Aestivum L ◽  
Polyacrylamide Gel

The objective of our study was to determine the composition of high-molecular weight-glutenin subunits (HMW-GS) in 120 cultivars of common wheat (Triticum aestivum L.). Fourteen alleles and 34 allelic compositions were detected using sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The most frequent HMW-GS alleles at the Glu-A1, Glu-B1 and Glu-D1 loci were null (57.1%), 7+9 (43.3%) and 5+10 (61.9%), respectively. However, low-frequency HMW-GS alleles were also observed, such as 13+16, 20, 21, 7 and 18, encoded by the Glu-B1 locus, and 4+12, encoded by the Glu-D1 locus. The wheat–rye 1BL.1RS translocation was identified in 25 cultivars, using acid polyacrylamide gel electrophoresis. The Glu-score varied greatly, and some lines reached the maximum value of 10.

scholarly journals THE USE OF SEED PROTEIN BANDING PATTERNS FOR IDENTIFICATION OF PASTURE CULTIVARS

1988 ◽  
pp. 87-91
Author(s):  
M.B. Forde ◽  
S.E. Gardiner
Keyword(s):  
Gel Electrophoresis ◽  
Seed Protein ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Subterranean Clover ◽  
Seed Storage Proteins ◽  
Polyacrylamide Gel ◽  
Banding Patterns ◽  
Seed Certification ◽  
Plant Variety

Because of the growing number of pasture cultivars used in NZ and the difficulty of reliably separating cultivars of the same species by morphological characters, seed protein banding patterns have become a useful supplementary means of cultivar identification for the purposes of seed certification and plant variety rights applications. Sodium dodecylsufphate polyacrylamide gel electrophoresis of proteins extracted from ground seed samples produces distinctive patterns of bands representing seed storage proteins of different molecular weights. The procedure can be carried out in two days using viable or dead seed, and the results are not affected by site and season of growth. Although individual seeds of outbreeding species such as perennial ryegrass and white clover produce different banding patterns, the combined population representing the cultivar remains constant unless there has been genetic shift during seed multiplication. Speckes for whrch this procedure is being successfully used include the ryegrasses and fescues, browntop, cocksfoot, bromes, red and white clovers, subterranean clover, serradella and lotus. Even cultrvars as closely related as Nui and Ellett ryegrasses and Huia and Pitau white clovers can be separated by careful work. Because of minor technical differences between runs, all cultivars to be compared must be run on the same gel. Keywords: Seed certification, Plant variety rights, sodium dodecylsulphate polyacrylamide gel electrophoresis.

Application of chromosome-specific monoclonal antibodies in wheat genetics

Genome ◽  
1992 ◽  
Vol 35 (5) ◽  
pp. 831-837 ◽  
Author(s):  
R. E. Knox ◽  
N. K. Howes ◽  
T. Aung
Keyword(s):  
Monoclonal Antibodies ◽  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Polyacrylamide Gel ◽  
Root Tip ◽  
Chromosome Marker

A monoclonal antibody (P24B) to a wheat gliadin protein coded by a gene on the short arm of chromosome 1B was used as a chromosome marker. Somatic chromosome number for the 1B chromosome, as predicted by the level of binding of the antibody to extracts from seeds of single cross F2 and testcross F1 populations, was confirmed with sodium dodecyl sulfate – polyacrylamide gel electrophoresis and root-tip analysis. The implications of monoclonal antibodies as tools for cytogenetic analysis are discussed.Key words: polyacrylamide gel electrophoresis, aneuploid, cytogenetics, seed storage proteins.

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.

Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Xa ◽  
Polyacrylamide Gel ◽  
Cleavage Pattern ◽  
Purification And Characterization ◽  
Double Immunodiffusion ◽  
The Family

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.

Functional Relationship of Polymerization Sites of Vertebrate Fibrinogens

1979 ◽  
Author(s):  
C Cierniewski ◽  
T Krajewski ◽  
E Janiak
Keyword(s):  
Gel Electrophoresis ◽  
Functional Relationship ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Functional Similarity ◽  
Fractionation Method ◽  
Relationship Of ◽  
Fibrin Monomers ◽  
Fibrinogen Molecule ◽  
Cold Ethanol Fractionation

Various studies on the interaction of immobilized mammalian fibrinogen and fibrin monomers with some fibrinogen derivatives demonstrated the presence of two sets of polymerization sites in the mammalian fibrinogen molecule. We obtained the same results while investigating the fibrinogen molecules of other classes of vertebrates /Pisces. Amphibia. Aves/. Despite significant differences among their subunit structures, all of them contain polymerization sites homologous to mammalian counterparts. Moreover, due to great functional similarity, fibrinogen or fibrin monomers of the analyzed species of Pisces. Amphibia. Aves and Mammalia interacted in a specific way with immobilized pig fibrin monomers or fibrinogen, respectively. Using these pig affinity adsorbents, fibrinogen and fibrin monomers of different vertebrates were isolated directly from plasma and analyzed by SDS polyacrylamide gel electrophoresis. Polypeptide compositions of eluted proteins were identical to those obtained for corresponding fibrinogen preparations isolated by cold-ethanol fractionation method. It appears to indicate that the nature of polymerization sites in vertebrate fibrinogens is alike.

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