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

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.

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Adaptation of the two-dimensional electrophoresis method for canned meat

IOP Conference Series Earth and Environmental Science ◽

10.1088/1755-1315/854/1/012001 ◽

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.

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Sialic Acid Dependent Polypeptide Chain Heterogeneity of Human Fibrinogen Demonstrated by Two-Dimensional Electrophoresis

Thrombosis and Haemostasis ◽

10.1055/s-0038-1657116 ◽

1982 ◽

Vol 47 (01) ◽

pp. 019-021 ◽

Cited By ~ 13

Author(s):

Cemal Kuyas ◽

André Haeberli ◽

P Werner Straub

Keyword(s):

Sialic Acid ◽

Polypeptide Chain ◽

Two Dimensional ◽

Charge Heterogeneity ◽

Human Fibrinogen ◽

Two Dimensional Electrophoresis ◽

Isoelectric Points ◽

Polypeptide Chains ◽

Dimensional Electrophoresis ◽

Chain Type

SummaryHuman fibrinogen was compared with asialofibrinogen by two-dimensional electrophoresis to evaluate the contribution of sialic acid to the heterogeneity of the γ- and Bβ-polypeptide chains.Reduced fibrinogen showed three major variants for both the γ- and Bβ-chains. In addition two minor γ-bands with a more acidic isoelectric point than the normal γ-chains were observed. Electrophoresis in the second dimension (SDS) suggests that these most acidic bands are γ-chain-variants with a higher molecular weight. In asialofibrinogen only two predominant variants with more alkaline isoelectric points were present in each chain type.It is concluded that enzymatic removal of sialic acid partially reduces the heterogeneity of the γ- and Bβ-polypeptide chains of human fibrinogen, but additional sources producing charge heterogeneity must be sought.

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Analytical electrofocusing and two-dimensional electrophoresis of proteins extracted from the mycelia of aggressive and nonaggressive strains of Ophiostoma ulmi

Canadian Journal of Botany ◽

10.1139/b86-272 ◽

1986 ◽

Vol 64 (9) ◽

pp. 2073-2081 ◽

Cited By ~ 10

Author(s):

Robert S. Jeng

Keyword(s):

Dutch Elm Disease ◽

Two Dimensional ◽

Polyacrylamide Gels ◽

Ophiostoma Ulmi ◽

Two Dimensional Electrophoresis ◽

Coomassie Blue ◽

Isoelectric Points ◽

Additional Protein ◽

Dimensional Electrophoresis ◽

Electrophoresis Of Proteins

Soluble mycelial proteins from Ophiostoma ulmi (Buism.) Nannf., the causal agent of Dutch elm disease, were separated by analytical electrofocusing and two-dimensional electrophoresis in polyacrylamide gels. Results showed the aggressive and nonaggressive strains of this pathogen each had about 60 Coomassie blue stained bands having isoelectric points from 3 to 7. Both strains of this fungus had their own characteristic electrofocusing patterns. Nonaggressive isolate S116, for example, lacked two protein bands, one near the anode and one near the cathode, but it had five additional protein bands distributed from pH 4 to 6. Two-dimensional electrophoresis of total soluble proteins depicted that there were 36 proteins found to be specific for the nonaggressive isolate S116 and 12 proteins for the aggressive isolate RR2.

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Plasma apolipoproteins in Tangier disease, as studied with two-dimensional electrophoresis.

Clinical Chemistry ◽

10.1093/clinchem/33.1.120 ◽

1987 ◽

Vol 33 (1) ◽

pp. 120-122 ◽

Cited By ~ 8

Author(s):

S Visvikis ◽

M F Dumon ◽

J Steinmetz ◽

T Manabe ◽

M M Galteau ◽

...

Keyword(s):

The Other ◽

High Density Lipoproteins ◽

Major Protein ◽

Two Dimensional ◽

Tangier Disease ◽

Two Dimensional Electrophoresis ◽

Isoelectric Points ◽

Molecular Masses ◽

Dimensional Electrophoresis ◽

Homozygous Patient

Abstract Tangier disease is characterized by a deficiency of high-density lipoproteins and of their major protein constituent, apolipoprotein (apo) A-I. We used high-resolution two-dimensional electrophoresis to examine the principal plasma apolipoproteins (A-I, A-II, A-IV, E, C-II, and C-III) of three persons with Tangier disease, one homozygous patient and his two heterozygous children, comparing the patterns with those for healthy subjects. Characteristic abnormalities were found in the distribution of the isoproteins of apo A-I, there being a normal concentration of pro apo A-I but dramatically decreased concentrations of the other apo A-I isoproteins. We also found hitherto-undescribed polypeptide abnormalities in apo C-III: sialylated and nonsialylated forms of apo C-III appear as double spots having the same isoelectric points but different molecular masses. No other substantial difference was detected in the polypeptide distribution of the other plasma apolipoproteins.

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Two-dimensional electrophoretic analysis of erythrocyte membranes.

Clinical Chemistry ◽

10.1093/clinchem/28.4.925 ◽

1982 ◽

Vol 28 (4) ◽

pp. 925-931 ◽

Cited By ~ 25

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.

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Variations in the Methionine-rich Protein Composition of the Genus Arachis1

Peanut Science ◽

10.3146/i0095-3679-11-1-1 ◽

1984 ◽

Vol 11 (1) ◽

pp. 1-3 ◽

Cited By ~ 3

Author(s):

Sheikh M. Basha ◽

Sunil K. Pancholy

Keyword(s):

Molecular Weight ◽

Gel Electrophoresis ◽

Protein Composition ◽

Electrophoretic Analysis ◽

Two Dimensional ◽

Weight Group ◽

Two Dimensional Gel Electrophoresis ◽

One Dimensional ◽

Molecular Weights ◽

Isoelectric Points

Abstract Methionine-rich proteins (MRP) from seeds of different species of the Genus Arachis were isolated and analyzed by gel electrophoresis to detect possible compositional differences. One-dimensional gel electrophoretic analysis showed presence of quantitative and qualitative variations among the MRP-fractions. Following two-dimensional gel electrophoresis, the MRP-fractions were found to contain three groups of polypeptides with apparent molecular weights of approximately 21,000; 19,000 and 16,000, and isoelectric points between 5.1 and 5.8. Within each molecular weight group the number of polypeptides varied between 1 and 3.

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Characterization of human blood platelet membrane proteins and glycoproteins by their isoelectric point (pI) and apparent molecular weight using two-dimensional electrophoresis and surface-labelling techniques

Biochimica et Biophysica Acta (BBA) - Biomembranes ◽

10.1016/0005-2736(80)90192-3 ◽

1980 ◽

Vol 599 (2) ◽

pp. 473-483 ◽

Cited By ~ 24

Author(s):

John L. McGregor ◽

Kenneth J. Clemetson ◽

Elizabeth James ◽

Ernst F. Luscher ◽

Marc Dechavanne

Keyword(s):

Molecular Weight ◽

Human Blood ◽

Apparent Molecular Weight ◽

Blood Platelet ◽

Two Dimensional ◽

Two Dimensional Electrophoresis ◽

Human Blood Platelet ◽

Surface Labelling ◽

Dimensional Electrophoresis

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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

Canadian Journal of Genetics and Cytology ◽

10.1139/g86-010 ◽

1986 ◽

Vol 28 (1) ◽

pp. 76-83 ◽

Cited By ~ 27

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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