The biased reptation model of DNA gel electrophoresis: Mobility vs molecular size and gel concentration

Biopolymers ◽  
1989 ◽  
Vol 28 (10) ◽  
pp. 1781-1791 ◽  
Author(s):  
Gary W. Slater ◽  
Jaan Noolandi
Keyword(s):  
Gel Electrophoresis ◽  
Molecular Size ◽  
Reptation Model

scholarly journals Immunochemical evidence for an additional H-2 region closely linked to H-2D.

1977 ◽  
Vol 145 (2) ◽  
pp. 438-442 ◽  
Author(s):  
T H Hansen ◽  
S E Cullen ◽  
D H Sachs
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Spleen Cell ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Molecular Size ◽  
Migration Patterns ◽  
Different Types ◽  
D Region ◽  
Chemical Evidence

Anti-H-2 reagents have been tested on solubilized spleen cell preparations in combinations expected to be specific for D region products. Two different types of molecules were detected. One showed the expected reactivity with both antisera to private and antisera to public specificities. However, an additional molecule was detected which reacted only with antisera to public specificities. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis migration patterns indicated that both products have a similar molecular size of approximately 45,000 daltons. The data therefore present chemical evidence for the existence of a third H-2-associated gene product of 45,000 mol wt in addition to the classical H-2K and H-2D antigens.

scholarly journals Evidence for two homologous, but nonidentical, Ia molecules determined by the I-EC subregion.

1979 ◽  
Vol 150 (1) ◽  
pp. 100-107 ◽  
Author(s):  
T L Delovitch ◽  
B H Barber
Keyword(s):  
Staphylococcus Aureus ◽  
Gel Electrophoresis ◽  
Peptide Mapping ◽  
Molecular Size ◽  
Gene Products ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Partial Digestion

Sequential immunoprecipitation, two-dimensional gel electrophoresis and peptide mapping analyses of B10A(3R), 35S-methionine-labeled, I-EC subregion products were performed. Evidence is presented here for the presence of two structurally homologous, but nonidentical, gene products of the I-EC subregion. These two Ia molecules are independently immunoprecipitable, identical in molecular size and charge, but differ by approximately equal to 20% in their peptides obtained by partial digestion with Staphylococcus aureus protease V8.

scholarly journals The molecular size of N-methylglutamate dehydrogenase of Pseudomonas aminovorans

1977 ◽  
Vol 167 (2) ◽  
pp. 509-512 ◽  
Author(s):  
C W Bamforth ◽  
P J Large
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein A ◽  
Sodium Dodecyl ◽  
Molecular Size ◽  
Partial Specific Volume ◽  
Triton X

N-Methylglutamate dehydrogenase, purified to a specific activity of 0.29 unit/mg of protein, gave one band on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, corresponding to a molecular weight of 130 000. Enzyme-Triton complexes were found to have a partial specific volume of 0.73 cm3/g, suggesting that the protein binds less than 0.1 g of Triton/g of protein. A molecular weight for the intact enzyme in the presence of 1% (w/v) Triton X-100 of 550 000 suggested that the enzyme may be a tetramer.

scholarly journals Conjugation of horseradish peroxidase to staphylococcal protein A with benzoquinone, glutaraldehyde, or periodate as cross-linking reagents.

1981 ◽  
Vol 29 (2) ◽  
pp. 266-270 ◽  
Author(s):  
H Nygren ◽  
H A Hansson
Keyword(s):  
Horseradish Peroxidase ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein A ◽  
Molecular Size ◽  
High Yield ◽  
Second Step ◽  
Cross Linking ◽  
Staphylococcal Protein A ◽  
Staphylococcal Protein

Horseradish peroxidase was conjugated to Staphylococcal protein A by three different two-step procedures using an increasing excess of peroxidase in the second step reaction. The yield of conjugated protein A was analyzed by SDS-polyacrylamide gel electrophoresis. Conjugation of peroxidase to protein A with benzoquinone or glutaraldehyde as cross-linking reagents at a 3- to 4-fold molar excess of peroxidase resulted in a high yield of coupled protein A with conjugates of low molecular size. Conjugation of peroxidase to protein A by the periodate method resulted in a high yield of coupled protein A with polymeric conjugates of large molecular size. Based on these results, conjugates produced with glutaraldehyde as cross-linking reagents were further analyzed. The capacity of the conjugates to precipitate human immunoglobulin evaluated by radial immunodiffusion was found to be reduced to about 50% of that of native protein A. Conjugates produced with glutaraldehyde as cross-linking reagent retained 70% of the enzyme activity of native peroxidase.

Soluble Crosslinked Fibrin(ogen) Polymers

1985 ◽  
Vol 54 (04) ◽  
pp. 804-807 ◽  
Author(s):  
Eberhard Selmayr ◽  
Gert Müller-Berghaus
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Gel Electrophoresis ◽  
Molecular Size ◽  
Density Gradients ◽  
Reducing Conditions ◽  
Diagnostic Criterion

SummaryThe present study is concerned with the formation of fibrin-fibrinogen associations in the presence of FXIIIa while fibrinolysis was inhibited by aprotinin and EACA. SDS agarose-poly acryl-amide gel electrophoresis on 2.5% gels under non-reducing conditions and ultracentrifugation of the associations on urea-sucrose density gradients showed the formation of soluble crosslinked high molecular weight (HMW) fibrin-fibrinogen polymers with an estimated molecular size up to 10 times that of fibrinogen. After incubation of a mixture of 131I-fibrinogen (4 mg/ml) and 125I-desAA-fibrin (0.2 mg/ml) with FXIIIa (2 U/ml) for 1 h at 37ΰ C, about 5% of the fibrinogen and 80% of the fibrin was incorporated into the generated soluble HMW polymers. The detection of soluble crosslinked fibrin-fibrinogen polymers could be a useful diagnostic criterion for imminent DIC.

Detection of Low Molecular Size Lipopolysaccharide Contaminated in Dialysates used for Hemodialysis Therapy with Polyacrylamide Gel Electrophoresis in the Presence of Sodium Deoxycholate

1993 ◽  
Vol 16 (5) ◽  
pp. 245-248 ◽  
Author(s):  
T. Komuro ◽  
R. Nakazawa
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Aqueous Media ◽  
Molecular Size ◽  
Sodium Deoxycholate ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Bacterial Endotoxin ◽  
Molecular Sizes ◽  
Dialysis Membranes

Dialysis membranes are generally considered to be impermeable for bacterial endotoxin (lipopolysaccharide, LPS) contaminated in dialysates used for hemodialysis therapy, since LPS molecular size in aqueous media has been reported to be more than 106. However, there are few reports concerning its size in dialysates. We have already presented a newly developed polyacrylamide gel electrophoresis with sodium deoxycholate (DOC-PAGE) which proves the LPS size. Using this method, therefore, we attempted to clarify the size of LPS in dialysates. We demonstrated that LPS in dialysates had roughly two different molecular sizes with DOC-PAGE and that compared to migration profiles of Salmonella LPS as controls on DOC-PAGE, one molecular size of LPS was approximately 4,000 and the other in tens of thousands. This investigation indicates the possibility of LPS transfer across dialysis membranes.

Characterization of group A streptococcal M-proteins purified by two methods

1976 ◽  
Vol 22 (8) ◽  
pp. 1072-1082
Author(s):  
David C. Straus ◽  
Charles F. Lange
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Molecular Size ◽  
M Protein ◽  
M Proteins ◽  
Group A ◽  
Terminal Amino ◽  
High Concentrations

Ten different group A streptococcal M-protein preparations purified by trichloroacetic acid precipitation and three M-protein preparations purified by cellulose chromatography were examined by SDS and polyacrylamide gel electrophoresis, and analyzed for amino acid composition and N-terminal amino acids. Fingerprinting (both tryptic and chymotryptic) was performed on the cellulose-purified preparations of M1, M12, and M29 proteins which showed these proteins to be structurally related. Trypsin produced maps with 37 to 42 peptides, whereas chymotrypsin digestion resulted in 8 to 12 peptides, depending on the M-type. Sequencing was performed on the M12 protein and tentative identification of nine N-terminal amino acids was made. Molecular weights of the cellulose and TCA-purified M-proteins were determined by SDS gel electrophoresis and chromatography on G-200 Sephadex, with comparable results, indicating molecular size of at least 23 000. The amino acid analyses of the 10 TCA-purified proteins followed the patterns established for M-proteins, with high concentrations of lysine, aspartic acid, glutamic acid, alanine, and leucine. All 10 proteins had L-alanine as their N-terminal amino acid. Evidence for a one way cross-reaction between type 1 and type 29 streptococci was also found.

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