Horizontal two-dimensional (iso-dalt) electrophoresis: Use of agarose isoelectric focusing and SDS gel electrophoresis in an exponential gradient for characterization of plasma proteins

1980 ◽  
Vol 1 (3-4) ◽  
pp. 159-163 ◽  
Author(s):  
David L. Emerson ◽  
Colette Chapuis-Cellier ◽  
Philippe Arnaud
Keyword(s):  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Two Dimensional

scholarly journals Mammalian mitochondrial ribosomes: Characterization of ribosomal proteins by two-dimensional gel electrophoresis

FEBS Letters ◽  
1976 ◽  
Vol 62 (3) ◽  
pp. 259-262 ◽  
Author(s):  
Winfried Czempiel ◽  
Joachim Klose ◽  
Rolf Bass
Keyword(s):  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Mitochondrial Ribosomes

Two-dimensional polyacrylamide gel electrophoresis map of bull seminal plasma proteins

1998 ◽  
Vol 19 (5) ◽  
pp. 797-801 ◽  
Author(s):  
Michele Mortarino ◽  
Gabriella Tedeschi ◽  
Armando Negri ◽  
Fabrizio Ceciliani ◽  
Luciano Gottardi ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Two Dimensional ◽  
Seminal Plasma Proteins

Proteomic Analysis by Two-Dimensional Gel Electrophoresis and Starch Characterization of Triticum turgidum L. var. durum Cultivars for Pasta Making

2008 ◽  
Vol 56 (18) ◽  
pp. 8619-8628 ◽  
Author(s):  
Maria De Angelis ◽  
Fabio Minervini ◽  
Leonardo Caputo ◽  
Angela Cassone ◽  
Rossana Coda ◽  
...  
Keyword(s):  
Proteomic Analysis ◽  
Gel Electrophoresis ◽  
Triticum Turgidum ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

scholarly journals Adición de proteínas del plasma seminal ovino durante la congelación del espermatozoide y efectos sobre su motilidad y viabilidad

2009 ◽  
Vol 10 (1) ◽  
pp. 51 ◽  
Author(s):  
Jaime Antonio Cardozo ◽  
Patricia Grasa ◽  
María Teresa Muiño B. ◽  
José Álvaro Cebrián P.
Keyword(s):  
Membrane Protein ◽  
Sperm Motility ◽  
Seminal Plasma ◽  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Two Dimensional ◽  
Plasma Séminal ◽  
Sperm Membrane ◽  
Seminal Plasma Proteins ◽  
Ram Sperm

<p>Este estudio se adelantó para evaluar el efecto de la adición de proteínas del plasma seminal de cordero en la criopreservación sobre la motilidad e integridad de la membrana espermática, y los cambios en el perfil electroforético de las proteínas de la membrana espermática inducidos por la criopreservación. Se usaron eyaculados de ocho corderos adultos de la raza rasa aragonesa, se les determinó su viabilidad y motilidad espermáticas y posteriormente se sometieron a un procedimiento de congelación. Las proteínas se separaron por el método de electroforesis en geles de acrilamida en dos dimensiones. Se obtuvo un mejoramiento significativo (<em>p </em>&lt; 0,05) en la calidad del semen congelado, cuando se adicionaron proteínas del plasma seminal. El análisis bidimensional comparativo entre el semen fresco y el congelado evidenció la pérdida de 8 puntos de proteína en el espermatozoide descongelado. La concentración de un punto de proteína de membrana espermática, de bajo peso molecular (punto 2), fue más alta (<em>p </em>&lt; 0,05) en el espermatozoide descongelado al que se adicionaron proteínas del plasma seminal. Se encontraron correlaciones entre algunos puntos de proteína y la motilidad y viabilidad espermáticas, lo cual sugiere que pueden jugar papeles importantes en el mantenimiento de la integridad y funcionalidad del espermatozoide. Se puede concluir que la adición de proteínas del plasma seminal en la congelación mejora la integridad del espermatozoide descongelado, y que la criopreservación del semen de cordero produce variaciones en la composición de las proteínas de membrana.  </p><p> </p><p><strong>Effect of seminal plasma proteins at freezing on ram sperm motility and viability</strong>  </p><p>The aim of the study was to evaluate the cryoprotective effect of seminal plasma proteins on ram sperm motility, membrane integrity and the changes in the profile of ram sperm membrane proteins induced by cryopreservation. Fresh ejaculates from 8 mature Rasa aragonesa rams were used. Sperm motility and cell viability was assessed. The freezing procedure was based on the method described by Fiser <em>et al</em>. (1987). Proteins extracted from fresh and frozen-thawed semen were subjected to the Two-dimensional polyacrilamide gel electrophoresis. A significant improvement in the quality of frozenthawed sperm was obtained after addition of seminal plasma proteins (<em>p </em>&lt; 0.05). Comparative two-dimensional polyacrilamide gel electrophoresis analysis between fresh and frozen semen, either with or without seminal plasma proteins in the cryopreservation medium, revealed that eight protein spots were lost in frozen-thawed sperm. The concentration of one sperm membrane protein spot of low Mr (spot 2) was higher (<em>p </em>&lt; 0.05) in proteinadded frozen sperm. Correlations found between certain protein spots sperm motility and viability suggests that these proteins could play important roles in the maintenance of sperm integrity and functionality. In conclusion, the addition of seminal plasma proteins to freezing extender improved frozen-thawed ram sperm integrity quality and cryopreservation of ram semen produced variations in the sperm membrane protein composition. </p>

Apolipoprotein C-II deficiency associated with nonfunctional mutant forms of apolipoprotein C-II

1984 ◽  
Vol 62 (9) ◽  
pp. 847-852 ◽  
Author(s):  
Graham F. Maguire ◽  
J. Alick Little ◽  
Gary Kakis ◽  
W. Carl Breckenridge
Keyword(s):  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Normal Subjects ◽  
Two Dimensional ◽  
Antibody Technique ◽  
Molecular Weights ◽  
Apolipoprotein C ◽  
Antigen Antibody ◽  
Mutant Forms

Two previously unidentified apolipoproteins (apo) designated apo C-II-X and C-II-Y have been found in plasma of homozygotes and obligate heterozygotes of a family with apo C-II deficiency. Because the plasmas of homozygotes do not activate lipoprotein lipase, apo C-II-X and C-II-Y are apparently nonfunctional. These apolipoproteins have isoelectric focusing points of 5.15 and 5.54, respectively, compared with 4.88 and 4.74 for the known isomorphs, C-II-1 and C-II-2, respectively. They have approximately similar molecular weights to apo C-II-1 and C-II-2 on two-dimensional sodium dodecyl sulphate – glycerol – polyacrylamide slab gel electrophoresis. They do not form insoluble antigen–antibody complexes with antibodies to apo C-II in single antibody immunodiffusion or electroimmunoassay systems. However, using a double-antibody technique in which immunoblotting is coupled with polyacrylamide isoelectric focusing slab gel electrophoresis, apo C-II-1, C-II-2, C-II-X, and C-II-Y have similar reactivity with antibodies to apo C-II. In this family the presence of apo C-II-X and C-II-Y discriminates obligate heterozygotes from normal subjects.

scholarly journals Purification and characterization of three forms of glutathione transferase from Proteus mirabilis

1988 ◽  
Vol 255 (3) ◽  
pp. 971-975 ◽  
Author(s):  
C Di Ilio ◽  
A Aceto ◽  
R Piccolomini ◽  
N Allocati ◽  
A Faraone ◽  
...  
Keyword(s):  
Amino Acid ◽  
Isoelectric Focusing ◽  
Proteus Mirabilis ◽  
Gel Electrophoresis ◽  
Glutathione Transferase ◽  
Total Activity ◽  
Purification And Characterization ◽  
Substrate Specificities ◽  
Structural Differences

Three forms of glutathione transferase (GST) with pI values of 6.0, 6.4 and 7.3 were isolated from Proteus mirabilis AF 2924 by glutathione-affinity chromatography followed by isoelectric focusing, and their structural, kinetic and immunological properties were investigated. Upon SDS/polyacrylamide-slab-gel electrophoresis, all forms proved to be composed of two subunits of identical (22,500) Mr. GST-6.0 and GST-6.4 together account for about 95% of the total activity, whereas GST-7.3 is present only in trace amounts. Extensive similarities have been found between GST-6.0 and GST-6.4. These include subunit molecular mass, amino acid composition, substrate specificities and immunological characteristics. GST-7.3 also cross-reacted (non-identity) with antisera raised against bacterial GST-6.0. None of the antisera raised against a number of human, rat and mouse GSTs cross-reacted with the bacterial enzymes, indicating major structural differences between them and the mammalian GSTs. This conclusion is further supported by c.d. spectra.

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