Quantitative characterization of specific genomic promoters using agarose gel electrophoresis

Biopolymers ◽  
2003 ◽  
Vol 68 (4) ◽  
pp. 557-562 ◽  
Author(s):  
Philippe T. Georgel ◽  
Jeffrey C. Hansen
Keyword(s):  
Gel Electrophoresis ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Quantitative Characterization

scholarly journals Performance Comparison of Capillary and Agarose Gel Electrophoresis for the Identification and Characterization of Monoclonal Immunoglobulins

2008 ◽  
Vol 129 (3) ◽  
pp. 451-458 ◽  
Author(s):  
Christopher R. McCudden ◽  
Stephanie P. Mathews ◽  
Shirley A. Hainsworth ◽  
John F. Chapman ◽  
Catherine A. Hammett-Stabler ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Performance Comparison ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Monoclonal Immunoglobulins ◽  
Identification And Characterization

Characterization of eight VNTR loci by agarose gel electrophoresis

Genomics ◽  
1989 ◽  
Vol 5 (4) ◽  
pp. 915-924 ◽  
Author(s):  
S.J. Odelberg ◽  
R. Plaetke ◽  
J.R. Eldridge ◽  
L. Ballard ◽  
P. O'Connell ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis

Rapid detection and characterization of plant virused by agarose gel electrophoresis: Size, surface charge and heterogeneity of panicum mosaic and related viruses

1984 ◽  
Vol 5 (4) ◽  
pp. 202-208 ◽  
Author(s):  
Philip Serwer ◽  
Elena T. Moreno ◽  
Shirley J. Hayes ◽  
Philip Berger ◽  
Marie Langham ◽  
...  
Keyword(s):  
Surface Charge ◽  
Gel Electrophoresis ◽  
Rapid Detection ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis

Characterization of Recombinant von Willebrand Factors Mutated on Cysteine 509 or 695

1996 ◽  
Vol 76 (03) ◽  
pp. 453-459 ◽  
Author(s):  
Virginie Siguret ◽  
Anne-Sophie Ribba ◽  
Olivier Christophe ◽  
Ghislaine Chérel ◽  
Bernadette Obert ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Mutant Proteins ◽  
Von Willebrand ◽  
High Molecular Weight Multimers

SummaryThe interacting domain of vWF with platelet GPIb has been shown to overlap the large A1 loop formed by the intra-chain disulfide bond linking Cys 509 to Cys 695. In order to further investigate the role of the conformation of this region, we have expressed in COS-7 cells three mutated full-length recombinant vWFs (rvWFs) in which the substitutions Cys509Gly, Cys509Arg or Cys695Gly have been introduced by site-directed mutagenesis. SDS-agarose gel electrophoresis demonstrated an impaired multimerization of the mutants with undetectable high molecular weight multimers and a decrease of the relative amounts of the intermediate sized multimers. Binding analysis showed that rvWFC509G and rvWFC509R did not interact with botrocetin but spontaneously interacted with GPIb; the latter binding remained unchanged in the presence of ristocetin. This indicates that the substitution of Cys509 by Gly or Arg creates a conformation of vWF that increases its binding to GPIb. In contrast, rvWFC695G which did not react with botrocetin was also unable to interact with GPIb even in the presence of ristocetin, indicating that sequences interacting with GPIb are masked and/or disrupted. In conclusion, the substitution of each of the Cys509 and 695 results in mutant proteins which may be “locked” into active or inactive conformations in regard to the binding to platelet GPIb receptor.

Applicability of agarose gel electrophoresis to the physical characterization of clathrin-coated vesicles

1985 ◽  
Vol 147 (2) ◽  
pp. 353-363 ◽  
Author(s):  
Melvin H. Gottlieb ◽  
Clifford J. Steer ◽  
Alasdair C. Steven ◽  
Andreas Chrambach
Keyword(s):  
Gel Electrophoresis ◽  
Coated Vesicles ◽  
Physical Characterization ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis

scholarly journals Characterization of Plasmids from Antibiotic-resistant Shigella Isolates by Agarose Gel Electrophoresis

1979 ◽  
Vol 113 (1) ◽  
pp. 73-81 ◽  
Author(s):  
A. F. Jamieson ◽  
D. A. Bremner ◽  
P. L. Bergquist ◽  
H. E. D. Lane
Keyword(s):  
Gel Electrophoresis ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Antibiotic Resistant

scholarly journals Purification and characterization of hyaluronic acid from chicken combs

2012 ◽  
Vol 42 (9) ◽  
pp. 1682-1687 ◽  
Author(s):  
Claudia Severo da Rosa ◽  
Ana Freire Tovar ◽  
Paulo Mourão ◽  
Ricardo Pereira ◽  
Pedro Barreto ◽  
...  
Keyword(s):  
Hyaluronic Acid ◽  
Gel Electrophoresis ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Purification And Characterization ◽  
Tissue Fractionation ◽  
Subsequent Identification

Hyaluronic acid (HA) is an important macromolecule in medical and pharmaceutical fields. The umbilical cord and the chicken comb are some of the tissues richest in this polysaccharide. The profit from obtaining HA from the combs of slaughtered animals is particularly attractive. This work aimed to extract, purify, and characterize HA. The glycosaminoglycan concentration in the chicken comb was found to be about 15µg of hexuronic acid mg-1 of dry tissue. Fractionation using ion exchange chromatography and subsequent identification of the fractions by agarose gel electrophoresis showed that HA corresponded to 90% of the total amount of extracted glycosaminoglycans.

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