Chromosomal assignment of genes coding for the wheat gliadin protein components of the cultivars ‘Cheyenne’ and ‘Chinese Spring’ by two-dimensional (two-pH) electrophoresis

1984 ◽  
Vol 68 (6) ◽  
pp. 531-539 ◽  
Author(s):  
D. Lafiandra ◽  
D. D. Kasarda ◽  
R. Morris
Keyword(s):  
Chinese Spring ◽  
Chromosomal Assignment ◽  
Two Dimensional ◽  
Wheat Gliadin ◽  
Protein Components ◽  
Gliadin Protein

Protein composition of nuclear matrix preparations from HeLa cells: an immunochemical approach

1986 ◽  
Vol 80 (1) ◽  
pp. 103-122
Author(s):  
R. Verheijen ◽  
H. Kuijpers ◽  
P. Vooijs ◽  
W. van Venrooij ◽  
F. Ramaekers
Keyword(s):  
Nuclear Matrix ◽  
Connective Tissue Diseases ◽  
Protein Composition ◽  
Cytoskeletal Proteins ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Core Proteins ◽  
Nuclear Rna ◽  
Hela S3 ◽  
Protein Components

Procedures for the isolation of HeLa S3 nuclear matrices were re-examined with special emphasis on the use of various nucleases and detergents as well as on the ionic strength of the final salt extraction. The protein composition of the resulting nuclear matrix preparations was analysed by one- and two-dimensional gel electrophoresis and found to be extremely reproducible. By means of co-electrophoresis several typical cytoskeletal proteins (actin, vimentin and cytokeratins) and heterogeneous nuclear RNA (hnRNA)-associated core proteins (hnRNP) were shown to be present in such nuclear matrix preparations. The nature of some other protein components was elucidated using two-dimensional immunoblotting and immunofluorescence. For this purpose mouse monoclonal antibodies to cytoskeletal components (vimentin, cytokeratins), small nuclear RNP (70 X 10(3) Mr protein of U1-RNP), hnRNP (C1/C2) and the pore-complex lamina (lamins A, B and C) were used next to human autoimmune sera obtained from patients with connective tissue diseases and directed against the residual nucleoli and the internal fibrillar mass. These antibodies enabled us to identify a number of proteins present specifically in the nuclear matrix and to show that part of the cytoskeletal proteins are still present in the isolated structures.

Two-dimensional electrophoretic analysis of erythrocyte membranes.

1982 ◽  
Vol 28 (4) ◽  
pp. 925-931 ◽  
Author(s):  
B B Rosenblum ◽  
S M Hanash ◽  
N Yew ◽  
J V Neel
Keyword(s):  
Erythrocyte Membrane ◽  
Polyacrylamide Gel Electrophoresis ◽  
Electrophoretic Analysis ◽  
High Molecular Mass ◽  
Erythrocyte Membranes ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Protein Components ◽  
Erythrocyte Membrane Proteins ◽  
Dimensional Electrophoresis

Abstract In an effort to maximize the amount of genetic information that can be extracted from a blood sample, we investigated the use of two-dimensional polyacrylamide-gel electrophoresis (PAGE) to resolve the protein constituents of the erythrocyte membrane. Lyophilized membranes were dissolved in various concentrations of urea, NP-40 detergent, and mercaptoethanol and subjected to two-dimensional PAGE by a modification of the O'Farrell procedure, with use of the ISO-DALT apparatus. More than 600 spots were visible in silver-stained gels under conditions that excluded specific cytoskeleton protein components, including spectrin and actin. The reproducibility of the pattern depended highly on the precise composition of the solubilization mixture. Poor resolution was observed in the presence of actin and other proteins of high molecular mass (spectrin bands 1 and 2) when we used high urea concentrations that solubilized the entire erythrocyte membrane. The large number of polypeptides observed could not be attributed to proteolysis, because addition of proteolytic inhibitors to the membrane wash solutions did not alter the pattern on the gel. The pattern also did not appear to include erythrocyte cytosol proteins because, except for globin, none of five purified erythrocyte lysate proteins was visible in the erythrocyte membrane gels. We conclude that two-dimensional electrophoresis provides a powerful tool for the study of non-cytoskeletal erythrocyte membrane proteins.

Chromosomal control of wheat gliadin protein epitopes: analysis with specific monoclonal antibodies

1991 ◽  
Vol 82 (1) ◽  
pp. 44-53 ◽  
Author(s):  
J. H. Skerritt ◽  
O. Martinuzzi ◽  
E. V. Metakovsky
Keyword(s):  
Monoclonal Antibodies ◽  
Wheat Gliadin ◽  
Gliadin Protein

Gliadin gene location and C-banding identification of Aegilops longissima chromosomes added to wheat

Genome ◽  
1991 ◽  
Vol 34 (2) ◽  
pp. 236-240 ◽  
Author(s):  
G. Hueros ◽  
J. M. Gonzalez ◽  
J. C. Sanz ◽  
E. Ferrer
Keyword(s):  
Gene Location ◽  
Addition Lines ◽  
Substitution Lines ◽  
Structural Modifications ◽  
C Banding ◽  
Aegilops Longissima ◽  
Gli 1 ◽  
Protein Components ◽  
Gliadin Protein ◽  
Alien Addition Lines

Gliadin protein components from Aegilops longissima were separated by two-dimensional electrophoresis. No equivalents for α-gliadin were noted. Addition and substitution lines of Ae. longissima in Triticum aestivum 'Chinese Spring' allowed the identification of homoeologous Gli-1 and Gli-2 loci in Ae. longissima chromosomes 1S1 and 6S1. The chromosomal constitution of the alien addition lines was ascertained by C-banding. In addition, C-banding analysis revealed that the Ae. longissima addition set was incomplete as only six distinct addition lines were identified. No evidence for structural modifications between the alien chromosomes in the lines and their Ae. longissima counterparts was found.Key words: gliadins, C-banding, gene location, Aegilops longissima, wheat.

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