scholarly journals Identification of Peanut Hybrids Using Microsatellite Markers and Horizontal Polyacrylamide Gel Electrophoresis

2008 ◽  
Vol 35 (2) ◽  
pp. 123-129 ◽  
Author(s):  
S. M. Gomez ◽  
N. N. Denwar ◽  
T. Ramasubramanian ◽  
Charles E. Simpson ◽  
G. Burow ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Leaf Tissue ◽  
Polyacrylamide Gel ◽  
Marker Allele ◽  
Breeding Programs ◽  
Banding Patterns ◽  
Use Of Resources ◽  
Effective Use ◽  
Band Separation

Abstract In peanut hybridization, distinguishing inadvertent selfs from the true hybrids may be difficult. In this study, to differentiate between selfs and hybrids, DNA was extracted from leaf tissue of F1 or F2 plants, and SSR markers were amplified and bands separated by a novel submarine horizontal polyacrylamide gel electrophoresis (H-PAGE). By comparing the resulting banding patterns to those of the parents, 70% of the putative hybrids were shown to be true hybrids on the basis of possessing a marker allele from the male parent. The H-PAGE gels gave better band separation and differentiation of selfed progenies than agarose gels, and were compatible with the common horizontal agarose gel units. This method provides a quick assay to distinguish hybrids from inadvertent selfs, and should result in greater efficiency and more effective use of resources in peanut breeding programs.

Electrophoretic evidence supporting self-incompatibility in Lotus corniculatus

1980 ◽  
Vol 58 (6) ◽  
pp. 712-716 ◽  
Author(s):  
Shirley Dobrofsky ◽  
W. F. Grant
Keyword(s):  
Gel Electrophoresis ◽  
Seed Set ◽  
Polyacrylamide Gel Electrophoresis ◽  
Lotus Corniculatus ◽  
Polyacrylamide Gel ◽  
Self Incompatibility ◽  
Banding Patterns ◽  
Protein Subunits ◽  
Self Pollination

Self-incompatibility, a prefertilization event, and self-sterility, a postfertilization event, have both been suggested as causes for differences in seed set between cross- and self-pollinated florets in Lotus corniculatus L. Ovary protein subunits of selfed, crossed, and unpollinated florets of L. corniculatus cv. Mirabel were studied using polyacrylamide gel electrophoresis. Banding patterns differed for all three conditions. Ovary protein differences were found prior to the time fertilization is known to occur, thereby providing evidence that self-incompatibility is at least partially responsible for the reduced seed set after self-pollination.

Isozymes as markers for identification of tissue culture and greenhouse-grown strawberry cultivars

1991 ◽  
Vol 71 (4) ◽  
pp. 1195-1201 ◽  
Author(s):  
N. S. Nehra ◽  
K. K. Kartha ◽  
C. Stushnoff
Keyword(s):  
Tissue Culture ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Meristem Culture ◽  
Banding Patterns ◽  
Extraction Buffer ◽  
Leaf Tissues ◽  
The Stability ◽  
Strawberry Cultivars

Polyacrylamide gel electrophoresis (PAGE) was used for analysis of isozyme banding patterns of leucine aminopeptidase (LAP), phosphoglucomutase (PGM), phosphoglucoisomerase (PGI), esterase (EST) and 6-phosphogluconate dehydrogenase (6-PGD) in strawberry leaves. The extracts prepared from young leaf tissues using polytron homogenization and an extraction buffer containing 15 mg ml−1 dithiothreitol (DTT) and 10% insoluble polyvinylpyrrolidone (PVP-6755) gave best resolution for these enzymes. The influence of plant age and various growing environments on the stability of isozyme phenotypes was examined. The isozyme banding patterns of 6-PGD were found to vary with the change in growing environment as well as age of the plants. EST produced different banding patterns in greenhouse and tissue culture leaves. However, the isozyme phenotypes of LAP, PGM and PGI remained stable under all the conditions tested. Using a combination of these three stable enzymes, it was possible to distinguish eight strawberry cultivars under both tissue culture and greenhouse conditions. Key words: Fragaria × ananassa Duch., meristem culture, polyacrylamide gel electrophoresis

Analysis of extracellular proteins by native polyacrylamide gel electrophoresis with infiltrated leaf tissue: application to pathogenesis-related proteins

1988 ◽  
Vol 66 (6) ◽  
pp. 1227-1229 ◽  
Author(s):  
Jean Grenier ◽  
François Côté ◽  
Alain Asselin
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Leaf Tissue ◽  
Polyacrylamide Gel ◽  
Simple Method ◽  
Pathogenesis Related Proteins ◽  
Intercellular Fluid ◽  
Pathogenesis Related ◽  
Native Polyacrylamide Gel Electrophoresis ◽  
Related Proteins

In addition to polyacrylamide gel electrophoretic analysis of intercellular fluid extracts, a simple method of detection of extracellular pathogenesis-related proteins was based on direct native polyacrylamide gel electrophoresis for acidic and basic proteins with leaf tissue infiltrated with 150 mM sucrose. This technique allowed for the detection of the complete set of tobacco pathogenesis-related proteins without having to extract the intercellular fluid by low-speed centrifugation. A major advantage of the technique is the capacity to observe the distribution of extracellular endogenous or exogenous proteins in the tissue directly subjected to electrophoresis.

Detection of 10 additional pathogenesis-related (b) proteins in intercellular fluid extracts from stressed 'Xanthi-nc' tobacco leaf tissue

1987 ◽  
Vol 65 (3) ◽  
pp. 476-481 ◽  
Author(s):  
Richard Hogue ◽  
Alain Asselin
Keyword(s):  
Gel Electrophoresis ◽  
Stress Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Leaf Tissue ◽  
Polyacrylamide Gel ◽  
Basic Proteins ◽  
Pathogenesis Related Proteins ◽  
Intercellular Fluid ◽  
Pathogenesis Related ◽  
Related Proteins

By using two-dimensional polyacrylamide gel electrophoresis, 10 additional pathogenesis-related proteins (b6c, b9c, b10a, b10b, b11a, b11b, b12, b13, b14, b15) were found in intercellular fluid extracts of stressed 'Xanthi-nc' tobacco leaf tissue. Proteins were identified as extracellular pathogenesis-related stress proteins by polyacrylamide gel electrophoresis analysis of three successive intercellular fluid extracts compared with homogenates before and after making intercellular fluid extracts. Four proteins (b12, b13, b14, b15) were only resolved by using native polyacrylamide gel electrophoresis for basic proteins in the first dimension gel and they were best extracted in 0.05 M Tris–HCl (pH 7.5) and 0.05 M CaCl2 as the infiltration buffer. The four basic proteins were found in intercellular fluid extracts from leaf tissue subjected to the same types of chemical inducers as previously described for tobacco pathogenesis-related proteins. Their accumulation was inhibited by basic amino acids or spermidine (1 mM) and they were resistant to endogenous and exogenous (trypsin, subtilisin) proteolysis. They did not bind to concanavalin A – Sepharose. These findings indicate that at least 23 proteins accumulate extracellularly after various types of stress in 'Xanthi-nc' tobacco green tissue. These proteins probably represent several groups or families of plant stress proteins.

GENETICS OF GLOSSINA MORSITANS MORSITANS (DIPTERA: GLOSSINIDAE): IV. ELECTROPHORETIC BANDING PATTERNS OF OCTANOL DEHYDROGENASE AND ARGININE PHOSPHOKINASE

1979 ◽  
Vol 111 (11) ◽  
pp. 1307-1310 ◽  
Author(s):  
R.H. Gooding ◽  
B.M. Rolseth
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Aldehyde Oxidase ◽  
Glossina Morsitans Morsitans ◽  
Polyacrylamide Gel ◽  
Single Locus ◽  
Single Individual ◽  
Glossina Morsitans ◽  
Banding Patterns ◽  
Octanol Dehydrogenase

AbstractPolyacrylamide gel electrophoresis of the thoraces of adult Glossina morsitans morsitans Westwood revealed five octanol dehydrogenase (ODH, E.C. 1.1.1.73) phenotypes (and a sixth was predicted) in males and females, two arginine phosphokinase (APK, E.C. 2.7.3.3) phenotypes in males and three APK phenotypes in females. Each enzyme was postulated to be under the control of a single locus; Odh with three alleles on an autosome and Apk with two alleles on the X-chromosome. Allele frequencies were in Hardy-Weinberg equilibrium in our colony, and breeding experiments provided direct evidence for single locus control of each enzyme. The polyacrylamide gel electrophoresis technique described permits determination of banding patterns for xanthine oxidase, aldehyde oxidase, ODH, and APK from a single individual.

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.

scholarly journals Lens neutral endopeptidase occurs in other bovine and human tissues

1987 ◽  
Vol 248 (3) ◽  
pp. 643-648 ◽  
Author(s):  
K Ray ◽  
H Harris
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Structural Difference ◽  
Double Diffusion ◽  
Neutral Endopeptidase ◽  
Relative Activity ◽  
Polyacrylamide Gel ◽  
Human Tissues ◽  
Banding Patterns ◽  
Bovine Lens

Lens neutral endopeptidase (EC 3.4.24.5) was previously thought to be unique to the eye lens. We report here the finding of a neutral endopeptidase, in a variety of bovine and human tissues, which is very similar both biochemically and immunologically to the lens endopeptidase. SDS/polyacrylamide-gel electrophoresis of partially purified enzyme fractions from various bovine tissues shows the characteristic pattern of at least eight bands with Mr values ranging from 24,000 to 32,000 which was described for the bovine-lens neutral endopeptidase. The relative activity of the enzyme varies from tissue to tissue with lung having the highest activity. Partially purified enzyme fractions from these tissues cross-react with antiserum raised in rabbit against bovine lens endopeptidase showing apparent identity when examined side by side in Ouchterlony double-diffusion tests. The human enzyme also cross-reacts with the antiserum but when tested by double-diffusion against the bovine enzyme the precipitin lines show spurring at the joining edges indicating a structural difference between the human and the bovine enzymes. It was also found by Western blot experiments, after denaturing polyacrylamide-gel electrophoresis of the enzyme, that the polypeptide components of the human and bovine enzymes show somewhat different banding patterns.

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).

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