Apparatus for automatic elution of wheat-protein fractions during starch-gel electrophoresis

1963 ◽  
Vol 14 (3) ◽  
pp. 175-179 ◽  
Author(s):  
G. A. H. Elton ◽  
J. A. D. Ewart
Keyword(s):  
Gel Electrophoresis ◽  
Protein Fractions ◽  
Starch Gel Electrophoresis ◽  
Wheat Protein ◽  
Starch Gel ◽  
Wheat Protein Fractions

scholarly journals Studies on Reduced Wool III. Starch-Gel Electrophoresis of Extracted Wool Proteins

1964 ◽  
Vol 17 (1) ◽  
pp. 277 ◽  
Author(s):  
EOP Thompson ◽  
IJ O'donnell
Keyword(s):  
Gel Electrophoresis ◽  
Moving Boundary ◽  
Electrophoretic Pattern ◽  
Deae Cellulose ◽  
Protein Fractions ◽  
Single Peak ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Wool Proteins

Starch-gel electrophoresis in 8M urea has been used to demonstrate the presence of many components in wool protein fractions extracted from reduced and alkylated wool. All preparations of low-sulphur wool proteins gave mUltiple bands on starch gel in 8M urea even though some of these had previously been fractionated to give a single peak using moving-boundary electrophoresis in the absence of 8M urea. The heterogeneity suggested by these results is in Rccord with that found by chromatography of the proteins on DEAE-cellulose in buffers containing 8M urea. With stepwise elution from DEAE-cellulose it is possible to obtain fractions responsible for various sections of the starch-gel electrophoretic pattern.

scholarly journals Properties of ribosomal proteins from two mammalian sources

1967 ◽  
Vol 102 (3) ◽  
pp. 735-741 ◽  
Author(s):  
P. Cohn
Keyword(s):  
Hydrochloric Acid ◽  
Glutamic Acid ◽  
Rat Liver ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Protein Fractions ◽  
Starch Gel Electrophoresis ◽  
Guanidinium Chloride ◽  
Starch Gel ◽  
Rabbit Reticulocytes

1. Ribosomal protein fractions from rabbit reticulocytes and rat liver were prepared by extracting ribosomes with 0.2n-hydrochloric acid or guanidinium chloride and subsequent dialysis. 2. Treatment for 2.5hr. or less with 0.2n-hydrochloric acid dissolved 46-54% of the proteins, which were richer in arginine and lysine and in N-terminal alanine groups and poorer in aspartic acid and glutamic acid and in N-terminal glycine groups than the acid-insoluble proteins. 3. Protein fractions prepared from the guanidinium chloride extract of ribosomes from rat liver were usually more basic than those from rabbit reticulocytes. 4. The ratios lysine: arginine of fractions in the guanidinium chloride extracts were appreciably higher for proteins from rabbit reticulocytes than from rat liver. 5. The concentration of urea and the pH of the gel affected the rate of migration and number of bands in starch-gel electrophoresis.

Abnormal protein fractions of cerebrospinal fluid demonstrated by starch gel electrophoresis

Neurology ◽  
1960 ◽  
Vol 10 (12) ◽  
pp. 1064-1064 ◽  
Author(s):  
H. Kutt ◽  
F. McDowell ◽  
L. Chapman ◽  
J. H. Pert ◽  
L. J. Hurwitz
Keyword(s):  
Cerebrospinal Fluid ◽  
Gel Electrophoresis ◽  
Protein Fractions ◽  
Starch Gel Electrophoresis ◽  
Abnormal Protein ◽  
Starch Gel

Fractionation of Plasminogen by Starch Gel Electrophoresis

1964 ◽  
Vol 12 (01) ◽  
pp. 126-136 ◽  
Author(s):  
Karl H. Slotta ◽  
J. D Gonzalez
Keyword(s):  
Gel Electrophoresis ◽  
Room Temperature ◽  
Broad Band ◽  
Caproic Acid ◽  
Starch Gel Electrophoresis ◽  
Full Activity ◽  
Veronal Buffer ◽  
Starch Gel ◽  
Alkaline Range

SummaryWhen urea or ε-amino caproic acid were used as solublizing agents for plasminogen in electrophoretic experiments, only one broad band of the proenzyme was obtained on acetate cellulose, in starch block, and in acrylamide gel. In starch gel electrophoresis, however, both forms of plasminogen – the native or euglobulin and Kline’s or Pseudoglobulin plasminogen – separated into six bands. These migrated toward the cathode at room temperature in borate or veronal buffer in the alkaline range and showed full activity in fibrinagar-streptokinase plates.

scholarly journals THE INHERITANCE OF ENZYME VARIANTS FOR TYROSINE AMINOTRANSFERASE, NADP-DEPENDENT MALATE DEHYDROGENASE, NADP-DEPENDENT ISOCITRATE DEHYDROGENASE, AND TETRAZOLIUM OXIDASE IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt
Keyword(s):  
Detailed Analysis ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Tyrosine Aminotransferase ◽  
Breeding Program ◽  
Starch Gel Electrophoresis ◽  
Enzyme Locus ◽  
Starch Gel

ABSTRACT The isozymic patterns of tyrosine aminotransferase, NADP malate dehydrogenase, NADP isocitrate dehydrogenase, and tetrazolium oxidase were examined by starch-gel electrophoresis in Tetrahymena pyriformis, syngen 1. The genetics of the alleles controlling these enzymes was studied through a breeding program. Each enzyme locus was shown to assort vegetatively, as do other loci in this organism. A detailed analysis of the assortment process for the tyrosine aminotransferase locus indicated that the rate of stabilization of heterozygotes into pure types was essentially identical to previously-reported rates for other loci.

STARCH GEL ELECTROPHORESIS OF MYOGEN FROM CHICKEN BREAST MUSCLE IN CONSTANT AND GRADIENT BUFFER SYSTEMS

1963 ◽  
Vol 41 (1) ◽  
pp. 369-387 ◽  
Author(s):  
J. M. Neelin
Keyword(s):  
Gel Electrophoresis ◽  
Protein Concentration ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Starch Gel Electrophoresis ◽  
Two Dimensional ◽  
Sodium Cacodylate ◽  
Gradient Systems ◽  
Optimal Separation ◽  
Starch Gel

By varying conditions of starch gel electrophoresis, factors contributing to the resolution of myogen proteins from chicken breast muscle have been studied. Variables examined included composition of the myogen extractant, protein concentration, ionic strength of electrophoretic media, pH of gel media, plane and direction of electrophoresis, and the nature of cations and anions in gel media and bridge solutions. The significance of anions was more closely studied with constant buffer systems, and gradient systems in which bridge electrolyte differed from, and gradually altered, the gel medium. Optimal separation was obtained in gradient systems with 0.10 M sodium chloride bridge solutions, and gel media of sodium cacodylate, pH 6.9, μ 0.010, which resolved 12 cationic zones, and sodium veronal, pH 7.4, μ 0.010, which resolved 10 anionic zones. These buffers in two-dimensional sequence revealed a total of about 24 components in this myogen.

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