scholarly journals Adaptation of the two-dimensional electrophoresis method for canned meat

2021 ◽  
Vol 854 (1) ◽  
pp. 012001
Author(s):  
V B Krylova ◽  
V T Gustova ◽  
A G Akhremko
Keyword(s):  
Molecular Weight ◽  
Two Dimensional ◽  
Molecular Weight Range ◽  
Two Dimensional Electrophoresis ◽  
Wide Range ◽  
Electrophoresis Method ◽  
Fat Removal ◽  
Canned Meat ◽  
Protein Components ◽  
Dimensional Electrophoresis

Abstract Studies of the qualitative indicators of canned meat in accordance with regulatory documents are carried out on average samples of specimens, but when studying by proteomic methods, such sampling does not allow high-quality separation of protein components due to the high fat content in the product. When two-dimensional electrophoresis was carried out on an average sample, fragments of the main muscle and connective tissue proteins of beef were found in small quantities, but the electrophoretogram was not very informative. A significantly better separation was achieved after removing the fat fraction from the product. When studying broth from canned meat, the largest amount of intensely coloured high-molecular-weight protein fractions with a mass of more than 50 kDa was revealed. The electrophoretogram of the meat pieces showed a wide range of proteins across the entire molecular weight range of the polyacrylamide gel, including major muscle proteins. The study of broth together with meat pieces but after fat removal is optimal for the primary screening of the protein component of canned meat.

The oral apparatus of Tetrahymena. V. Oral apparatus polypeptides and their distribution

1980 ◽  
Vol 44 (1) ◽  
pp. 317-333
Author(s):  
R.H. Gavin
Keyword(s):  
Molecular Weight ◽  
Basal Body ◽  
Tetrahymena Thermophila ◽  
Electrophoretic Analysis ◽  
Two Dimensional ◽  
Molecular Weight Range ◽  
Two Dimensional Electrophoresis ◽  
Weight Range ◽  
Isoelectric Points ◽  
Dimensional Electrophoresis

Two-dimensional electrophoresis was used to resolve approximately 162 polypeptides from the isolated oral apparatus of Tetrahymena thermophila. The molecular weight range was between 110 000 and 15 000 Daltons. The polypeptides had apparent isoelectric points between pH 3.3 and pH 7.2. Electrophoretic analysis of isolated ciliary axonemes and fractionated oral apparatuses made possible the assignment of polypeptides to structures within the oral apparatus. Approximately 24 polypeptides, including alpha and beta tubulins, are probable components of the basal body-basal plate complex. At least 5 of the oral apparatus polypeptides, including alpha and beta tubulin, are components of the oral apparatus ciliary axonemes. Approximately 138 polypeptides are components of the oral apparatus framework.

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.

Two-dimensional electrophoresis method used for determination of plasmid profiles of Escherichia coli isolated from a sewage treatment plant

1993 ◽  
Vol 39 (10) ◽  
pp. 990-993 ◽  
Author(s):  
M. Arturo ◽  
Z. Tamanai-Shacoori ◽  
C. Mamez ◽  
M. Pommepuy ◽  
M. Cormier
Keyword(s):  
Escherichia Coli ◽  
Brackish Water ◽  
Sewage Treatment ◽  
Sewage Treatment Plant ◽  
Treatment Plant ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Treated Sewage ◽  
Electrophoresis Method ◽  
Dimensional Electrophoresis

The plasmid contents of 306 strains of Escherichia coli isolated from raw and treated sewage from a treatment plant as well as from the water 1 km downstream were determined. The number and molecular weight of plasmids isolated from a representative sample of these strains were also measured. It was observed that biological treatment did not significantly alter these parameters. In contrast, statistically significant differences in plasmid number and size were observed when strains from sewage (raw and treated) were compared with strains isolated from brackish water. In raw and treated sewage, more than 96% of the strains contained plasmids, compared with 85% in brackish water. Nine to 13% of the strains from sewage contained plasmids with more than 56 kilobases, while only 5% of the strains from brackish water reached this size.Key words: Escherichia coli, plasmids, two-dimensional electrophoresis, sewage treatment, brackish water.

Chromosomal locations of the structural genes for secalins in wild perennial rye (Secale montanum Guss.) and cultivated rye (S. cereale L.) determined by two-dimensional electrophoresis

1986 ◽  
Vol 28 (1) ◽  
pp. 76-83 ◽  
Author(s):  
P. R. Shewry ◽  
S. Parmar ◽  
N. Fulrath ◽  
D. D. Kasarda ◽  
T. E. Miller
Keyword(s):  
Molecular Weight ◽  
Storage Proteins ◽  
Seed Proteins ◽  
Relative Molecular Mass ◽  
Two Dimensional ◽  
Structural Genes ◽  
Substitution Lines ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis ◽  
Secale Montanum

The chromosomal locations of the structural genes for secalin storage proteins in Secale cereale and S. montanum were determined by electrophoresis of grain proteins from wheat–rye addition and substitution lines. The use of several different extraction procedures and high-resolution electrophoretic systems (one and two dimensional) enabled us to demonstrate that the genes for all the high molecular weight secalins are present on chromosome IRL, and for all the ω-secalins and at least some of the γ-secalins with a relative molecular mass (Mr) of 40 000 on chromosome IRS of both species. In contrast, the genes for the γ-secalins (Mr = 75 000) are located on 2RcS in S. cereale but 6Rm in S. montanum. These observations are discussed in relation to evolution of prolamins and their genes in Secale and related members of the Triticeae.Key words: Secale, rye, seed proteins, structural genes, two-dimensional electrophoresis.

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