INFLUENCE OF ALIEN GENOME COMBINATIONS ON PROTEIN SYNTHESIS IN CEREALS

1964 ◽  
Vol 42 (12) ◽  
pp. 1647-1657 ◽  
Author(s):  
F. C. Yong ◽  
A. M. Unrau
Keyword(s):  
Protein Synthesis ◽  
Gel Electrophoresis ◽  
Triticum Durum ◽  
Tetraploid Wheat ◽  
Water Soluble ◽  
Starch Gel Electrophoresis ◽  
Triticum Vulgare ◽  
Qualitative And Quantitative ◽  
Starch Gel ◽  
Variable Influence

Starch-gel electrophoresis of the water-soluble, salt-soluble, and alcohol soluble proteins of Triticale, Triticum durum, Secale cereale, Triticum vulgare, and Tritipyron revealed both qualitative and quantitative differences. The experimental evidence obtained indicated that the biosynthetic potential of the alien genomes in the synthetic species (Triticale) was not fully maintained. A variable influence of the tetraploid wheat (T. durum) genomes on protein synthesis in the three hexaploid cereals (Triticale, T. vulgare, and Tritipyron) was observed.

Identification of Australian barley cultivars by laboratory methods: gel electrophoresis and gel isoelectric focusing of the endosperm proteins

1977 ◽  
Vol 17 (89) ◽  
pp. 1020 ◽  
Author(s):  
J McCausland ◽  
CW Wrigley
Keyword(s):  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Water Soluble ◽  
The Other ◽  
Starch Gel Electrophoresis ◽  
Laboratory Methods ◽  
Barley Cultivars ◽  
Starch Gel ◽  
Electrophoretic Techniques ◽  
Gel Isoelectric Focusing

A range of laboratory methods was examined for their ability to distinguish between 19 barley cultivars currently grown in Australia. Aleurone colour, revealed after mechanical or chemical dehulling, differentiated Abyssinian, Atlas, Cape and Corvette from the other cultivars. Peroxidase and phenol testing were not useful. Seven different patterns were obtained for the hordeins of lowest mobility by starch gel electrophoresis. Further distinction was provided by flat gel isoelectric focusing of the water-soluble and hordein proteins for which 13 different pattern-groupings were obtained. The two electrophoretic techniques complemented one another, so that the use of both methods left only a few cultivars that could not be distinguished.

scholarly journals Methods for starch-gel electrophoresis of sarcoplasmic proteins. An investigation of the relative mobilities of the glycolytic enzymes from the muscles of a variety of species

1968 ◽  
Vol 107 (2) ◽  
pp. 139-150 ◽  
Author(s):  
R. K. Scopes
Keyword(s):  
Filter Paper ◽  
Enzyme Activities ◽  
Gel Electrophoresis ◽  
Detailed Comparison ◽  
Water Soluble ◽  
Starch Gel Electrophoresis ◽  
Muscle Proteins ◽  
Improved Method ◽  
Sarcoplasmic Proteins ◽  
Starch Gel

1. Details of an improved method for starch-gel electrophoresis of water-soluble muscle proteins are given. 2. Methods are described for detecting enzyme activities on the starch gel after electrophoresis, by using pieces of filter paper. 3. Compositions of incubation mixtures suitable for detecting any of the enzymes of glycolysis, and certain other enzymes, are given. 4. A comparison of the various enzymes in extracts of several muscles from one rabbit was made; most differences are quantitative only. 5. A detailed comparison of the mobilities of various enzymes in extracts of muscles from a wide variety of species was made. Each species was found to have a characteristic pattern of proteins on the starch gel, and the mobilities of individual enzymes varied considerably. 6. Potential uses and extensions of the methods are discussed.

CHARACTERIZATION OF THE ESTERASES FROM ELECTRIC TISSUE OF ELECTROPHORUS BY STARCH-GEL ELECTROPHORESIS

1967 ◽  
Vol 45 (7) ◽  
pp. 1099-1105 ◽  
Author(s):  
D. J. Ecobichon ◽  
Y. Israel
Keyword(s):  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Water Soluble ◽  
Starch Gel Electrophoresis ◽  
Electrophorus Electricus ◽  
Vertical Zone ◽  
Zone Electrophoresis ◽  
Starch Gel

The water-soluble esterases of a microsome-free supernatant of the electric tissue of Electrophorus electricus were separated by vertical-zone electrophoresis in starch gel. Specific and nonspecific substrates and inhibitors were used in conjunction with histochemical techniques to identify the enzymes. Acetylcholinesterase was present in the form of four bands of activity, the electrophoretic mobility of which was suggestive of aggregated forms of the enzyme. Pseudocholinesterase was detected as two weak bands of activity. A third esterase was identified as a nonspecific carboxylesterase and shown to be a sialoprotein.

scholarly journals Starch Gel Electrophoresis of Basic Water-Soluble Barley Grain Proteins.

1962 ◽  
Vol 16 ◽  
pp. 517-518 ◽  
Author(s):  
Tor-Magnus Enari ◽  
Juhani Mikola ◽  
Martti Nummi ◽  
T. Norin ◽  
G. A. D. Haslewood ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Barley Grain ◽  
Water Soluble ◽  
Starch Gel Electrophoresis ◽  
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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