scholarly journals Genetic variability among cassava accessions based on SSR markers

2011 ◽  
Vol 11 (3) ◽  
pp. 263-269 ◽  
Author(s):  
Márcia de Nazaré Oliveira Ribeiro ◽  
Samuel Pereira de Carvalho ◽  
João Bosco dos Santos ◽  
Rafaela Priscila Antonio
Keyword(s):  
Cluster Analysis ◽  
Gel Electrophoresis ◽  
Genetic Similarity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Dna Amplification ◽  
Microsatellite Primers ◽  
Hybrid Generation ◽  
Dice Coefficient ◽  
Expected Heterozygosity ◽  
Heterotic Hybrid

The aim of this study was to characterize and estimate the genetic similarity among 93 cassava accessions. The DNA amplification was performed with 14 microsatellite primers. The amplification products were separated by a polyacrylamide gel electrophoresis, showing a polymorphism formation, through which the accessions were discriminated against. The genetic similarity among accessions of cassava was estimated by the Dice coefficient. Cluster analysis was carried out using the UPGMA method. The polymorphic primers amplified a total of 26 alleles with 2-4 alleles per loci. The genetic similarity ranged from 0.16 to 0.96. The average values for observed and expected heterozygosity were 0.18 and 0.46, respectively. Twenty genetic similarity clusters were determined, demonstrating diversity among accessions, suggesting the possibility of heterotic hybrid generation.

scholarly journals Haemophilus influenzaesubtyping by SDS-PAGE of whole-cell polypeptides

1987 ◽  
Vol 99 (1) ◽  
pp. 179-189 ◽  
Author(s):  
A. J. Paterson ◽  
K. F. Macsween ◽  
T. H. Pennington
Keyword(s):  
Haemophilus Influenzae ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Type B ◽  
Dice Coefficient ◽  
Whole Cell ◽  
Coomassie Blue ◽  
Sds Page

SUMMARYStrains ofHaemophilus influenzaeisolated from patients in N.E. Scotland between 1983 and 1986 have been subtyped by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) of whole-cell polypeptides. Gels were stained with Coomassie blue and polypeptide profiles were analysed using the Dice coefficient of similarity.Type b strains were all closely related, the 19 strains analysed being grouped at a 90% similarity level into one large (13 strains) and one small (3 strains) cluster with 3 strains being ungrouped. Thirty-six non-typable, epidemiologically unrelated strains were subtyped; one pair of strains had indistinguishable polypeptide profiles. The polypeptide profiles of the remaining strains showed much heterogeneity, although groups of strains isolated from the same patient over short periods showed indistinguishable profiles.

scholarly journals Isoenzyme polymorphism of almond genotypes selected in the region of northern Serbia

2010 ◽  
Vol 37 (No. 2) ◽  
pp. 56-61 ◽  
Author(s):  
S. Čolić ◽  
D. Milatović ◽  
D. Nikolić ◽  
G. Zec
Keyword(s):  
Cluster Analysis ◽  
Alkaline Phosphatase ◽  
Gel Electrophoresis ◽  
Malic Enzyme ◽  
Formate Dehydrogenase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Prunus Dulcis ◽  
Enzyme Systems ◽  
Isoenzyme Polymorphism ◽  
First Time

Isoenzyme polymorphism was studied in 20 almond (Prunus dulcis [Mill.] D.A. Webb) genotypes selected from seedling populations of unknown almond cultivars in the region of northern Serbia (Vojvodina). Fourteen enzyme systems were studied using the method of vertical polyacrylamide gel electrophoresis. Ten systems were polymorphic in twelve loci. This polymorphism allowed unique identification of all studied genotypes. The most useful enzyme for analysis of almond genetic variability was menadione reductase. Polymorphism identified for alkaline phosphatase, formate dehydrogenase, glutamate dehydrogenase, malic enzyme, and menadione reductase was reported for the first time in almond. Cluster analysis was used to construct a dendrogram on which five clusters with different number of genotypes could be identified.

scholarly journals Heterogeneity Studies of Wild Clarias gariepinus (Osteichthyes, Clariidae) Using SDS-Polyacrylamide Gel Electrophoresis

2018 ◽  
Vol 52 (6) ◽  
pp. 457-462
Author(s):  
F. A. Ola-Oladimeji ◽  
E. O. Idowu ◽  
A. A. Adewumi ◽  
K. C. Fafowora
Keyword(s):  
Cluster Analysis ◽  
Serum Protein ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Clarias Gariepinus ◽  
Natural Populations ◽  
Similarity Index ◽  
Protein Profiles ◽  
Standard Methods ◽  
Caudal Vein

Abstract This study determined the genetic variations that exist in Clarias gariepinus obtained from two natural populations in Nigeria, using their serum protein profiles. A total of 51 samples of Clarias gariepinus collected from Ado-Ekiti and Ilesa were used for this experiment. Blood was extracted from the caudal vein of each individual fish and electrophoresis was performed based on standard methods. Following this, gel images were taken, scored and subjected to classical cluster analysis using Bray-Curtis similarity index. This showed the presence of variations in C. gariepinus between the studied populations and samples from Ado-Ekiti reservoir displayed more diversity than those from Ilesa. Hence, this showed the feasibility for selecting samples from Ado- Ekiti to improve culture of C. gariepinus in further breeding studies.

scholarly journals Genetic Relationships among Weedy Purple Loosestrife (Lytrhum salicaria L.) Populations and Cultivars

HortScience ◽  
1995 ◽  
Vol 30 (4) ◽  
pp. 856F-856
Author(s):  
Mark S. Strefeler ◽  
Elizabeth Darmo ◽  
Roger L. Becker ◽  
Elizabeth J. Katovich
Keyword(s):  
Cluster Analysis ◽  
Gel Electrophoresis ◽  
Genetic Similarity ◽  
Genetic Relationships ◽  
Geographic Location ◽  
Purple Loosestrife ◽  
Starch Gel Electrophoresis ◽  
Plant Proteins ◽  
Perennial Plant ◽  
Starch Gel

Starch gel electrophoresis of plant proteins was used to genetically identify purple loosestrife (Lythrum spp.) cultivars and weedy populations. Preliminary determinations were made as to what degree weedy loosestrife populations were related (or genetically similar) to populations of L. alatum, L. virgatum, and horticultural cultivars. Cluster analysis of the data indicated that native L. alatum was genetically different from all populations of purple loosestrife and cultivars examined. The L. salicaria and L. virgatum cultivars, as groups, were not genetically distinguishable from the weedy populations analyzed. Seven cultivars of L. salicaria origin analyzed as a group were not distinguishable from the eight cultivars of L. virgatum origin, indicating that separation by cultivar origin may not be feasible. While the two “groups” were not distinguishable, most individual cultivars could be distinguished from one another by isozyme phenotype. Genetic variation was high within populations of weedy purple loosestrife but low among populations, which is characteristic of polyploid, perennial plant species that are widely distributed. Geographic location did not consistently correlate with genetic similarity.

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).

Isolation of Human Fibrinogen and its Derivatives by Affinity Chromatography on Gly-Pro-Arg-Pro-Lys-Fractogel

1990 ◽  
Vol 63 (03) ◽  
pp. 439-444 ◽  
Author(s):  
C Kuyas ◽  
A Haeberli ◽  
P Walder ◽  
P W Straub
Keyword(s):  
Gel Electrophoresis ◽  
Affinity Purification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ease Of Use ◽  
Terminal Sequence ◽  
Purification Method ◽  
Human Fibrinogen ◽  
Isolation Methods ◽  
One Step ◽  
Complementary Binding

SummaryWith an immobilized synthetic pentapeptide GlyProArgProLys comprising the N-terminal sequence GlyProArg of the α-chain of fibrin, a new affinity method for the quantitative isolation of fibrinogen out of anticoagulated plasma was developed. The method proved to be superior to all known isolation methods in respect to ease of use and yield, since fibrinogen could be isolated in one step out of plasma with a recovery of more than 95% when compared to the immunologically measurable amounts of fibrinogen. Moreover the amounts of contaminating proteins such as fibronectin, factor XIII or plasminogen were negligible and the purity of the isolated fibrinogen was higher than 95% as measured by polyacrylamide gel electrophoresis. The clottability was 90% and more. Another advantage of this affinity purification method is the possibility to isolate fibrinogen quantitatively out of small plasma samples (<5 ml). Further, abnormal fibrinogen molecules, provided their complementary binding site for GlyProArg is preserved, may also be quantitatively isolated independent of any solubility differences as compared to normal fibrinogen. In addition fibrin(ogcn) fragments originating from plasmic digestion can be separated on the basis of their affinity to GlyProArg. The described affinity gel can be used more than 50 times without any loss of capacity.

Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant

1992 ◽  
Vol 68 (05) ◽  
pp. 534-538 ◽  
Author(s):  
Nobuhiko Yoshida ◽  
Shingi Imaoka ◽  
Hajime Hirata ◽  
Michio Matsuda ◽  
Shinji Asakura
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Tetraacetic Acid ◽  
Fibrin Monomer ◽  
Sds Page ◽  
Thrombotic Tendency ◽  
Chain Variant

SummaryCongenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D1 of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D1 γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).

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