An evaluation of gradient acrylamide gel electrophoresis and acrylamide gel isoelectric focusing for the primary separation of complex mixtures of proteins: Comparison of one- and two-dimensional analytical procedures

1973 ◽  
Vol 295 (2) ◽  
pp. 396-411 ◽  
Author(s):  
G.L. Wright ◽  
K.B. Farrell ◽  
D.B. Roberts
Keyword(s):  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Complex Mixtures ◽  
Two Dimensional ◽  
Primary Separation ◽  
Analytical Procedures ◽  
Gel Isoelectric Focusing

Occurrence of five αs1-casein variants in ovine milk

1996 ◽  
Vol 63 (1) ◽  
pp. 49-59 ◽  
Author(s):  
Lina Chianese ◽  
Giuseppina Garro ◽  
Rosalba Mauriello ◽  
Pasquale Laezza ◽  
Pasquale Ferranti ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Electrospray Mass Spectrometry ◽  
Polyclonal Antibodies ◽  
Population Sample ◽  
Italian Population ◽  
Protein Chain ◽  
Two Dimensional ◽  
Gel Isoelectric Focusing

SummaryFive ovine αsl-casein variants (A–E) were identified in an Italian population sample using gel electrophoresis at alkaline pH, gel isoelectric focusing, two dimensional gel electrophoresis, and immunoblotting with polyclonal antibodies against αs1-casein. Each casein sample produced two peaks by fast reversed-phase HPLC. Gel isoelectric focusing and electrospray mass spectrometry were used to demonstrate that the first HPLC peak contained the 191 residue αsl-casein molecular species and the second the 199 residue species, in proportions of ∼20:80. Only in the case of the sample containing αsl-casein CE was the method for the separation of the single short and long forms of each variant unsuccessful. Both two dimensional electrophoresis followed by staining with polyclonal antibodies against αsl-casein and electrospray mass spectrometry showed a heterogeneity consistent with that expected from a protein chain with three levels of phosphorylation and two different lengths. However, especially for αsl-caseins D and E, a further uncharacterized heterogeneity was detected.

Identification of Australian barley cultivars by laboratory methods: gel electrophoresis and gel isoelectric focusing of the endosperm proteins

1977 ◽  
Vol 17 (89) ◽  
pp. 1020 ◽  
Author(s):  
J McCausland ◽  
CW Wrigley
Keyword(s):  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Water Soluble ◽  
The Other ◽  
Starch Gel Electrophoresis ◽  
Laboratory Methods ◽  
Barley Cultivars ◽  
Starch Gel ◽  
Electrophoretic Techniques ◽  
Gel Isoelectric Focusing

A range of laboratory methods was examined for their ability to distinguish between 19 barley cultivars currently grown in Australia. Aleurone colour, revealed after mechanical or chemical dehulling, differentiated Abyssinian, Atlas, Cape and Corvette from the other cultivars. Peroxidase and phenol testing were not useful. Seven different patterns were obtained for the hordeins of lowest mobility by starch gel electrophoresis. Further distinction was provided by flat gel isoelectric focusing of the water-soluble and hordein proteins for which 13 different pattern-groupings were obtained. The two electrophoretic techniques complemented one another, so that the use of both methods left only a few cultivars that could not be distinguished.

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.

Isoelectric Focusing and Two-Dimensional Gel Electrophoresis in Plasma and Cerebrospinal Fluid from Patients with Dementia

1986 ◽  
Vol 25 (4) ◽  
pp. 285-289 ◽  
Author(s):  
I. Alafuzoff ◽  
R. Adolfsson ◽  
G. Bucht ◽  
E. Jellum ◽  
P.D. Mehta ◽  
...  
Keyword(s):  
Cerebrospinal Fluid ◽  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis
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