Reduced polypeptides from Lincoln wool: sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, isoelectric focusing and two-dimensional electrophoresis

1985 ◽  
Vol 13 (1) ◽  
pp. 241-242 ◽  
Author(s):  
J. CHRISTOPHER HORN ◽  
PETER T. SPEAKMAN
Keyword(s):  
Isoelectric Focusing ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

scholarly journals Purification and properties of succinyl-coenzyme A-3-oxo acid coenzyme A-transferase from sheep kidney

1978 ◽  
Vol 173 (3) ◽  
pp. 759-765 ◽  
Author(s):  
J A Sharp ◽  
M R Edwards
Keyword(s):  
Isoelectric Focusing ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Coenzyme A ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sedimentation Coefficient ◽  
Polyacrylamide Gel ◽  
Transferase Activity ◽  
Coa Transferase

CoA-transferase (succinyl-CoA-3-oxo acid CoA-transferase, EC 2.8.3.5) isolated from sheep kidney was purified to homogeneity. The purified enzyme has a specific activity of approx. 200 units/mg. A mol.wt. of 110000 was obtained by gel filtration on Sephadex G-200, and a lower mol.wt. of 102000 was determined by analytical ultracentrifugation. A sedimentation coefficient of 5.6S was also determined. A subunit mol.wt. of 56000 was obtained by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Isoelectric focusing of sheep kidney extracts indicated the presence of a single band of CoA-transferase activity with pI9.0. However, isoelectric focusing of purified CoA-transferase showed the presence of two peaks of CoA-transferase activity with pI values of 8.7 and 8.4, suggesting the presence of proteolytic activity during purification. Evidence for sheep kidney CoA-transferase being a dimer of two identical subunits has been obtained from sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, the amino acid composition, peptide ‘mapping’ and N-terminal analysis.

scholarly journals A novel two-dimensional polyacrylamide-gel pattern, which may be due to allelic genes, of phenylalanine hydroxylase in monkeys

1985 ◽  
Vol 231 (1) ◽  
pp. 197-199 ◽  
Author(s):  
S C Smith ◽  
W McAdam ◽  
R G H Cotton ◽  
J F B Mercer
Keyword(s):  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Phenylalanine Hydroxylase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
The Novel ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Monkey Liver

Two-dimensional gel electrophoresis of immunopurified monkey liver phenylalanine hydroxylase showed a novel form of the enzyme, in 4 out of 24 monkeys, in which each polypeptide spot was split into a doublet with the same charge but slightly different mobility in the sodium dodecyl sulphate/polyacrylamide-gel-electrophoresis (as opposed to the isoelectric-focusing) dimension. Phenylalanine hydroxylase formed by translation of RNA from a liver containing the novel form showed the doublet pattern, suggesting that it is due to differences in mRNA. By analogy with the rat, this mRNA difference could be due to allelic genes.

Comparative study on polypeptide patterns of larvae of Trichinella isolates by two-dimensional electrophoresis

1987 ◽  
Vol 61 (3) ◽  
pp. 225-228 ◽  
Author(s):  
T. Garate ◽  
L. Rivas
Keyword(s):  
Comparative Study ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Polypeptide Patterns ◽  
Muscle Larvae ◽  
The Comparative Study ◽  
Dimensional Electrophoresis

ABSTRACTThe two-dimensional patterns (isoelectrofocusing-IEF/polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate-SDS) of S3 fractions of muscle larvae of four Trichinella isolates were compared. The comparative study concerned six groups of polypeptides. It was observed that the Garkavi isolate of Trichinella pseudospiralis was clearly different from the other isolates, and it showed the simplest IEF/SDS polypeptide pattern. The C-76 isolate of T. nelsoni had only four of the six groups, distinguishing it from the GM-1 isolate of T. spiralis and the Boev isolate of T. nativa that showed all the indicated groups.

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