Subunit structure of the 12S protein from seeds of Brassica juncea

1975 ◽  
Vol 53 (24) ◽  
pp. 2901-2907 ◽  
Author(s):  
S. L. MacKenzie
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Brassica Juncea ◽  
Acid Composition ◽  
Isoelectric Focusing ◽  
Electrophoretic Analysis ◽  
Subunit Structure ◽  
Isoelectric Points

The 12S globulin from Brassica juncea seeds has been dissociated by 6 M urea: 0.1 M mercaptoethanol and the resultant products have been partially separated by preparative isoelectric focusing. Species that have the isoelectric points 4.75, 5.15, 5.40, 6.25, 6.70, 7.00, 7.20, 7.70, 8.30, 8.90, and 9.15 were detected. The results of poly aery lamide-gel electrophoretic analysis and the amino acid composition of the fractions suggested that the isoelectric species were distinct subunits.

scholarly journals α1-Acute-phase globulins of rats. Microheterogeneity after isoelectric focusing

1972 ◽  
Vol 130 (1) ◽  
pp. 95-101 ◽  
Author(s):  
A. H. Gordon ◽  
P. J. Dykes
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Isoelectric Focusing ◽  
Isoelectric Points ◽  
Individual Bands ◽  
The Stability ◽  
The Individual ◽  
Gel Isoelectric Focusing

1. Improved resolution of mixtures of α1-globulins was obtained by the use of isoelectric focusing. 2. Because material recovered after isoelectric focusing in polyacrylamide gels behaved in a manner which suggested interaction with components derived from the gel, isoelectric focusing when used for preparative purposes was done in a matrix of Sephadex G-75. 3. By this means material from the individual bands formed by isoelectric focusing in 6m-urea could be isolated. The stability of these substances was examined by further isoelectric focusing. 4. Analysis of material that had been shown to be homogenous by isoelectric focusing in the absence of urea and of that from several individual bands derived from the same sample by isoelectric focusing in 6m-urea showed different proportions of sialic acid but no change in amino acid composition. 5. In the presence of 6m-urea the isoelectric points found were increased by 0.14–0.25 pH unit. After removal of most of the sialic acid with neuraminidase the increase was 0.36–0.72 pH unit. After treatment with 0.025m-H2SO4 at 80°C for 1h, which removed all the sialic acid, the increase was 0.40–0.87 pH unit. 6. Because removal of all the sialic acid did not decrease the number of bands formed by isoelectric focusing the observed heterogeneity could not be caused entirely by the presence of various proportions of sialic acid.

scholarly journals Ribitol dehydrogenase from Klebsiella aerogenes. Purification and subunit structure

1974 ◽  
Vol 141 (3) ◽  
pp. 693-700 ◽  
Author(s):  
Susan S. Taylor ◽  
Peter W. J. Rigby ◽  
Brian S. Hartley
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Subunit Structure ◽  
Klebsiella Aerogenes ◽  
Peptide Maps ◽  
Ribitol Dehydrogenase

Ribitol dehydrogenase has been purified to homogeneity from several strains of Klebsiella aerogenes. One strain yields 3–6g of pure enzyme from 1kg of cells. The enzyme is a tetramer of four subunits, mol.wt. 27000. Preliminary studies of the activity of the enzyme are reported. Peptide ‘maps’ together with the amino acid composition indicate that the subunits are identical.

scholarly journals Studies on Ovalbumin V. The Amino Acid Composition and Some Properties of Chicken, Duck, and Turkey Ovalbumins

1970 ◽  
Vol 23 (5) ◽  
pp. 1221 ◽  
Author(s):  
MB SmIth ◽  
Joan F Back
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Ammonium Sulphate ◽  
Acid Composition ◽  
Isoelectric Focusing ◽  
Ph Gradient ◽  
Ammonium Sulphate Fractionation

The ovalbumins from chicken, duck, and turkey eggs were prepared by ammonium sulphate fractionation and purified by isoelectric focusing in a pH gradient from 3 to 6. Amino acid analyses show a closer relationship between turkey and chicken ovalbumins than between duck and chicken ovalbumins.

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