scholarly journals An Improved Chromatographic Separation of Wheat Gluten Proteins

1965 ◽  
Vol 18 (1) ◽  
pp. 193 ◽  
Author(s):  
CW Wrigley
Keyword(s):  
Column Chromatography ◽  
Chromatographic Separation ◽  
Gel Electrophoresis ◽  
Carboxymethyl Cellulose ◽  
Wheat Gluten ◽  
Starch Gel Electrophoresis ◽  
Gluten Proteins ◽  
Electrophoretic Patterns ◽  
Starch Gel

Gel electrophoresis is at present the best procedure for the analytical fractiona-tion of wheat gluten proteins. Procedures more suitable for preparative studies, such as gel ffitration and column chromatography, have provided only partial fractionation on the basis of gel electrophoresis (Graham 1963; Lee et al. 1963; Wright, Brown, and Bell 1964). Gel electrophoretic patterns of fractions resulting from the carboxymethyl cellulose (CMC) fractionation of Simmonds and Winzor (1961) have been published by Graham (1963) and by Lee et al. (1963). These results showed that each fraction was heterogeneous, with considerable overlapping of electrophoretic bands from neighbouring fractions, and that fractions eluted late in the chromatogram were contaminated because of tailing of earlier fractions. The modification of the Simmonds and Winzor procedure described below results in an improved fractionation of gluten proteins as judged by starch-gel electrophoresis.

scholarly journals Erythrocyte glutathione S-transferase. Electrophoretic identification of two enzyme forms

1983 ◽  
Vol 215 (1) ◽  
pp. 213-216 ◽  
Author(s):  
R C Strange ◽  
P H Hirrell ◽  
G A Kitley ◽  
D A Hopkinson ◽  
W Cotton
Keyword(s):  
Enzyme Activity ◽  
Individual Differences ◽  
Gel Electrophoresis ◽  
Human Erythrocytes ◽  
Starch Gel Electrophoresis ◽  
Glutathione S Transferase ◽  
Electrophoretic Patterns ◽  
Starch Gel

Starch-gel electrophoresis was used to demonstrate two forms of glutathione S-transferase in human erythrocytes. Whereas considerable inter-individual differences in enzyme activity and electrophoretic patterns were detected, intra-individual differences were small.

Translation of protamine mRNA in a rabbit reticulocyte cell-free system

1977 ◽  
Vol 55 (2) ◽  
pp. 152-158 ◽  
Author(s):  
Lashitew Gedamu ◽  
Gordon H. Dixon
Keyword(s):  
Gel Electrophoresis ◽  
Carboxymethyl Cellulose ◽  
Starch Gel Electrophoresis ◽  
Stages Of Development ◽  
Free System ◽  
Cell Free System ◽  
Polyadenylated Rna ◽  
Starch Gel ◽  
Three Components

Protamine mRNA isolated from the microsomal and postribosomal supernatant fractions of trout testis in poly A(+) (polyadenylated RNA) and poly A(−) (RNA devoid of poly A(+)) forms (Gedamu, L. &Dixon, G.H. (1976)7. Biol. Chem. 251, 1446–1454 and 1455–1463) was translated in the heterologous rabbit reticulocyte cell-free system; the products were shown to be identical in mobility with authentic protamine by polyacrylamide and starch gel electrophoresis. Chromatography, on carboxymethyl cellulose (Whatman CM-52), of the labelled polypeptide products synthesized in this cell-free system in the presence of poly A(+) and poly A(−) mRNA fractions also showed that [14C]arginine was incorporated into all three protamine components resolved in this system, but there was an unequal and variable incorporation of label into the three components with different preparations of mRNA. These results were interpreted as showing that the population of subcomponents of the protamine mRNA coding for the three different protamine polypeptides varied in batches of trout testis at differing stages of development. In addition, the proportion of mRNA components varied between the poly A(+) and poly A(−) editions of the mRNA, and it appeared that the poly A(−) mRNA fraction might represent the product of deadenylation of an earlier population of poly A(+) mRNA.

scholarly journals Genetic variation in the triploids of Japanese Fasciola species, and relationships with other species in the genus

1994 ◽  
Vol 68 (3) ◽  
pp. 181-186 ◽  
Author(s):  
T. Agatsuma ◽  
K. Terasaki ◽  
L. Yang ◽  
D. Blair
Keyword(s):  
United States Of America ◽  
Gel Electrophoresis ◽  
Laboratory Strain ◽  
Morphological Type ◽  
The United States ◽  
Starch Gel Electrophoresis ◽  
Isozyme Patterns ◽  
Electrophoretic Patterns ◽  
Starch Gel ◽  
Liver Flukes

AbstractTwelve enzymes (encoded by 14 loci) in liver flukes of Fasciola species originating from Japan (parthenogenetic triploids), Korea (parthenogenetic diploids), the United States of America (USA) and Australia (all sexual diploids) were analysed using starch gel electrophoresis. Variation in electrophoretic patterns between samples was detected at five enzyme loci (Ak, Got, Gpi, 6-Pgd and Pgm-2). Japanese worms (31, of which six were established as uniparental laboratory strains), which reproduce by parthenogenesis, exhibited three different isozyme patterns. This indicates that triploidy has arisen more than once in Japanese flukes. Japanese Fasciola sp. can be separated into three types on morphological grounds. For the six laboratory strains of Japanese worms, the parental morphological type was known. Each of the three isozyme patterns observed was restricted to one morphological type. Most alleles detected in the Japanese triploids were also found in diploid worms from the other countries: the only alleles not represented elsewhere were four at the Got locus and two at the Pgm locus. Flukes from a laboratory strain derived from a single Korean diploid worm resembled the Japanese worms in genotype more closely than did American (seven uniparental laboratory strains) or Australian (30 worms) specimens. Worms from the last two countries were closely related.

CHARACTERISTIC ELECTROPHORETIC PATTERNS OF SERUM PROTEINS OF SEVERAL SPECIES OF SNAKES OF IRAN

1965 ◽  
Vol 43 (4) ◽  
pp. 459-461 ◽  
Author(s):  
M. Latifi ◽  
K. D. Shamloo ◽  
A. Amin
Keyword(s):  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Starch Gel Electrophoresis ◽  
Gel Method ◽  
Electrophoretic Patterns ◽  
Starch Gel

Paper and starch-gel electrophoresis of serum proteins of several species and subspecies of poisonous and nonpoisonous snakes of Iran have been investigated. The patterns obtained, especially by means of the starch-gel method, are characteristic for each species. Electrophoretic patterns of samples of serum from different individuals of the same species were very similar.

A COMPARISON OF HISTONES FROM CHICKEN TISSUES BY ZONE ELECTROPHORESIS IN STARCH GEL

1961 ◽  
Vol 39 (3) ◽  
pp. 485-491 ◽  
Author(s):  
J. M. Neelin ◽  
G. C. Butler
Keyword(s):  
Cell Differentiation ◽  
Ionic Strength ◽  
Gel Electrophoresis ◽  
The Other ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Patterns ◽  
Zone Electrophoresis ◽  
Starch Gel ◽  
Chicken Erythrocytes ◽  
Characteristic Zone

Histories were extracted at pH 1.7 from washed nuclei of chicken erythrocytes, spleen, liver, and testis and compared by starch-gel electrophoresis at pH 5.0, ionic strength 0.020. Spleen and liver histories displayed the most complex electrophoretic patterns with 18 zones each and differed only in relative proportions of certain zones. Erythrocyte histone contained a characteristic zone while lacking a group present in spleen and liver histones. Testis histone with only seven zones differed markedly from the other three. These results were consistent with chromatograms of erythrocyte, spleen, and liver histones on sodium IRC-50. The suggested correlation of tissue-specific histones with cell differentiation is discussed.

Ontogenetic Variation in the Multiple Hemoglobins of Coho Salmon (Oncorhynchus kisutch) and Effect of Environmental Factors on Their Expression

1976 ◽  
Vol 33 (5) ◽  
pp. 1144-1149 ◽  
Author(s):  
M. A. Giles ◽  
W. E. Vanstone
Keyword(s):  
Environmental Factors ◽  
Dissolved Oxygen ◽  
Gel Electrophoresis ◽  
Coho Salmon ◽  
Oncorhynchus Kisutch ◽  
Yolk Sac ◽  
Ontogenetic Variation ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Patterns ◽  
Starch Gel

Hemolyzates from the blood of coho salmon (Oncorhynchus kisutch) at various stages of development were subjected to micro-starch-gel electrophoresis. Three distinct electrophoretic patterns composed of different combinations of 18 hemoglobin tetramers were observed. Embryonic and yolk-sac alevins possessed 1 cathodic and 12 anodic components while fry retained only 3 of the 12 anodic polymorphs. During smoltification, 4 new cathodic components appeared and 2 of the anodic and the cathodic components of alevin hemolyzates reappeared. This latter pattern was retained until the fish spawned and died. Attempts to induce changes in the pattern of development of these hemoglobins by exposing fry and pre-smolts to extreme variations in dissolved oxygen, temperature, and salinity were completely unsuccessful.

Studies on the relation between plasma antithrombin and heparin-cofactor

1968 ◽  
Vol 46 (3) ◽  
pp. 347-350 ◽  
Author(s):  
F. C. Monkhouse ◽  
Susan Milojevic
Keyword(s):  
Gel Electrophoresis ◽  
Specific Activity ◽  
Deae Cellulose ◽  
Fold Increase ◽  
Significant Loss ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Patterns ◽  
Starch Gel ◽  
Cofactor Activity ◽  
Cellulose Column

A method for the preparation of purified plasma antithrombin and heparin-cofactor is described. The method involves adsorption by aluminium hydroxide, separation on a DEAE-cellulose column by means of a graded salt concentration, and vertical curtain electrophoresis. A 100-fold increase in the specific activity of antithrombin and a 30-fold increase in the specific activity of heparin-cofactor have been achieved. In spite of the increased purification, no separation of the two activities was achieved. When a highly purified fraction was subjected to starch-gel electrophoresis for 16–18 h and then eluted from the gel, there was significant loss of heparin-cofactor activity but not of antithrombin activity. The electrophoretic patterns of the recovered proteins were not altered.

Human Prothrombin

1970 ◽  
Vol 24 (03/04) ◽  
pp. 311-324 ◽  
Author(s):  
Th. R Derleth ◽  
J. A Penner
Keyword(s):  
Cellulose Acetate ◽  
Chromatographic Separation ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
High Specific Activity ◽  
Factor Ix ◽  
Factor Vii ◽  
Starch Gel Electrophoresis ◽  
Multiple Protein ◽  
Starch Gel

SummaryA method is presented for the chromatographic separation of human prothrombin from variable volumes of plasma. The procedure is simple, consisting of chromatography on ECTEOLA which provides a potent product containing factor IX and X activity sufficient for therapeutic use. Additional chromatography on DEAE or Sephadex G200 will produce a prothrombin of high specific activity which appears homogeneous by ultracentrifugation and electrophoresis on cellulose acetate, although multiple protein fractions can be identified on starch gel electrophoresis.Human prothrombin prepared by this method migrates as an alpha 2-globulin and does not appear to be altered electrophoretically or antigenically from its original state in the plasma. The characteristics of human prothrombin obtained from patients with deficiencies of factor VII or IX do not differ from normal.

On the validity of the genus Musculium (Bivalvia: Sphaeriidae): electrophoretic evidence

1980 ◽  
Vol 58 (9) ◽  
pp. 1703-1707 ◽  
Author(s):  
Daniel J. Hornbach ◽  
M. J. McLeod ◽  
S. I. Guttman
Keyword(s):  
Gel Electrophoresis ◽  
Habitat Characteristics ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Patterns ◽  
Enzyme Systems ◽  
Starch Gel ◽  
Phenotypic Convergence

Starch gel electrophoresis was used to examine the generic separation of the sphaeriid clams Musculium and Sphaerium. Twenty-five loci from 13 enzyme systems were resolved. Major differences in electrophoretic patterns were observed, and these appear to support the generic separation of Musculium and Sphaerium. Sphaerium occidentale, considered to be intermediate in form between Musculium and Sphaerium, is more closely related (electrophoretically) to other spieces of Sphaerium than to Musculium. The phenotypic convergence of S. occidentale with Musculium and its genotypic divergence from other species of Sphaerium can be related to habitat characteristics of these forms.

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