Comparison of Haemophilus Equigenitalis (Contagious Equine Metritis Organism) and Other Haemophilus Species by Disc Electrophoresis of Acid-Phenol-Soluble Proteins

1983 ◽  
Vol 139 (3) ◽  
pp. 200-203 ◽  
Author(s):  
R.A. Brewer ◽  
M.J. Corbel
Keyword(s):  
Soluble Proteins ◽  
Disc Electrophoresis ◽  
Contagious Equine Metritis ◽  
Haemophilus Species

Changes in soluble proteins of cinnamon fern leaves during development

1972 ◽  
Vol 50 (7) ◽  
pp. 1479-1483 ◽  
Author(s):  
James D. Caponetti ◽  
William H. Harvey ◽  
A. E. DeMaggio
Keyword(s):  
Soluble Proteins ◽  
Disc Electrophoresis ◽  
Flowering Plants ◽  
Leaf Primordia ◽  
Young Leaf ◽  
Apical Region ◽  
Mature Leaves ◽  
Fern Leaves

The complement of soluble proteins contained in the five annual leaf sets and the apical region of the shoot of cinnamon fern, Osmunda cinnamomea L., has been determined using disc electrophoresis. The apical region and the very young leaf primordia contained high and comparable numbers of soluble proteins. Older primordia and mature leaves contained progressively fewer soluble proteins, except that the number of proteins increased in the oldest sets of leaves. These findings are discussed in relation to the results reported for the leaves of some flowering plants.

SOLUBLE PROTEINS AND COLD HARDINESS OF TWO WOODY SPECIES

1969 ◽  
Vol 49 (3) ◽  
pp. 279-286 ◽  
Author(s):  
L. E. Craker ◽  
L. V. Gusta ◽  
C. J. Weiser
Keyword(s):  
Low Temperature ◽  
Moisture Content ◽  
Total Nitrogen ◽  
Cold Hardiness ◽  
Morphological Changes ◽  
Woody Species ◽  
Soluble Proteins ◽  
Disc Electrophoresis ◽  
Ionic Surfactant ◽  
Electrophoretic Patterns

A simplified, highly reproducible procedure is outlined for the extraction and polyacrylamide gel disc electrophoresis of acidic soluble proteins from apple bark and arborvitae foliage. The procedure includes low temperature maceration, short extraction time, and an extraction solution which contains polyol and phenolic complexers, a reducing agent, and a non-ionic surfactant. Electrophoretic patterns, total nitrogen, moisture content, minimum survival temperatures, and environmental and morphological changes were examined during the natural dehardening of apple and the controlled hardening of arborvitae. Qualitative protein changes, as evidenced by the appearance and disappearance of specific bands, occurred at times when changes in hardiness were taking place.

Egg and embryo proteins in European newts (genus Triturus) and their taxonomic potential

1987 ◽  
Vol 8 (3) ◽  
pp. 203-211
Author(s):  
Michael Veith
Keyword(s):  
Embryonic Development ◽  
Soluble Proteins ◽  
Disc Electrophoresis ◽  
Water Soluble ◽  
Diagnostic Studies ◽  
Triturus Alpestris ◽  
Tailbud Stage ◽  
Species Specific

AbstractPolyacrylamide disc electrophoresis was carried out on water soluble proteins of eggs and embryos of Triturus alpestris, T. boscai, T. cristatus, T. helveticus, T. marmoratus and T. vulgaris. "Major bands" and "minor bands" were defined and species specific phenotyps are described. The patterns of major bands proved to be rather constant during embryonic development up to approximately stage 30 (stretched tailbud stage). The method as used in this study is considered to be practical and relevant for diagnostic studies on Triturus species.

Disc electrophoresis of soluble proteins of conifer foliage

1970 ◽  
Vol 9 (11) ◽  
pp. 2281-2285 ◽  
Author(s):  
Eleanor E. McMullan ◽  
L.F. Ebell
Keyword(s):  
Soluble Proteins ◽  
Disc Electrophoresis

Über das Verhalten der in Acrylamid getrennten löslichen Proteine aus Erbsenwurzeln bei verlängerter Elektrophorese-Dauer / Behaviour of the soluble Proteins of Pea Roots under extended Electrophoresis in Acrylamide Gels

1969 ◽  
Vol 24 (9) ◽  
pp. 1180-1183 ◽  
Author(s):  
Conrad Polter ◽  
W. R. Müller-Stoll
Keyword(s):  
Developmental Stages ◽  
Soluble Proteins ◽  
Disc Electrophoresis ◽  
Protein Preparation ◽  
Seedling Roots ◽  
Pea Roots ◽  
Differentiation Stage ◽  
Protein Spectra ◽  
Pea Seedling

The soluble proteins from distinct sections of pea seedling roots, in different developmental stages, were separated by acrylamide disc-electrophoresis. Each time eight columns charged with the same protein preparation were separated simultaneously. Each column was subjected to electrophoresis seven minutes longer than the previous one. In this way the more quickly running protein bands left the columns step by step whereas the remaining ones broadened and in some cases split. In columns of the tip section only one new band was observed while those of the second section showed several new bands. The protein spectra of the differentiation stage of older root parts had the largest increase in number of bands. At present one can not decide wether the analogous bands from different root sections contain primarily different proteins or that the protein is oxidized at a different rate.

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