Two-Dimensional Electrophoretic Study of the Water-Soluble Protein Fraction in White Muscle of Gadoid Fish Species

1998 ◽  
Vol 46 (10) ◽  
pp. 3991-3997 ◽  
Author(s):  
C. Piñeiro ◽  
J. Barros-Velázquez ◽  
C. G. Sotelo ◽  
R. I. Pérez-Martín ◽  
J. M. Gallardo
Keyword(s):  
Fish Species ◽  
Soluble Protein ◽  
Protein Fraction ◽  
White Muscle ◽  
Water Soluble ◽  
Two Dimensional ◽  
Soluble Protein Fraction ◽  
Electrophoretic Study ◽  
Water Soluble Protein

Effect of age and temperature on amino acid composition and the content of different protein types of juvenile Atlantic cod (Gadus morhua) otoliths

2004 ◽  
Vol 61 (6) ◽  
pp. 1012-1020 ◽  
Author(s):  
K Hüssy ◽  
H Mosegaard ◽  
F Jessen
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Soluble Protein ◽  
Protein Fraction ◽  
Gadus Morhua ◽  
Atlantic Cod ◽  
Water Soluble ◽  
Soluble Protein Fraction ◽  
Water Soluble Protein

The purpose of this study was to analyse the amino acid composition of otolith matrix protein, estimate the proportion of the water-soluble protein fraction, and analyse the effect of matrix composition on otolith visual appearance. Juvenile Atlantic cod (Gadus morhua) were reared under constant temperature and feeding conditions and sampled at the beginning and the end of the experiment. The amino acid composition was dominated by asparagine, glutamic acid, leucine, serine, and proline. A change in amino acid composition was observed with increasing temperature and time, caused by changing proportions of the water-soluble and -insoluble protein fractions. Feeding level had no effect. The relative content of water-soluble protein was linearly related to fish dry weight and temperature. Otolith opacity, defined as the percentage of incident light absorbed by an otolith section, did not differ significantly between experimental treatments. The soluble protein fraction had a positive, albeit insignificant, correlation with opacity. Using opacity and otolith volume, deposited total otolith protein content was estimated with an R2 of 0.91, where otolith volume alone explained 83% of the observed variation.

scholarly journals ANTIBODY STUDIES IN RABBIT ENCEPHALOMYELITIS INDUCED BY A WATER-SOLUBLE PROTEIN FRACTION OF RABBIT CORD

1962 ◽  
Vol 116 (6) ◽  
pp. 807-825 ◽  
Author(s):  
Robert F. Kibler ◽  
Arthur E. Barnes
Keyword(s):  
Soluble Protein ◽  
Protein Fraction ◽  
Nervous Tissue ◽  
Serum Antibody ◽  
Paper Electrophoresis ◽  
Water Soluble ◽  
Soluble Protein Fraction ◽  
Water Soluble Protein ◽  
Antigen Antibody ◽  
Suitable Technique

A water-soluble protein fraction of nervous tissue was prepared by extraction of rabbit spinal cord with sodium citrate at pH 4.3. Characterization by nitrogen content and paper electrophoresis showed it to be a mixture of basic proteins. This extract demonstrated encephalitogenic activity when injected into rabbits. The most suitable technique for the measurement of serum antibody to the rabbit cord antigen proved to be the precipitation of antigen-antibody complexes by 40 per cent saturated ammonium sulfate. Antibody could not be demonstrated by the techniques of complement fixation, quantitative precipitation, and Ouchterlony plates. The early appearance of circulating antibody occurred almost exclusively in rabbits that subsequently developed EAE. Specificity of the antibodies for nervous tissue was demonstrated by appropriate blocking and adsorption experiments.

A trypsin inhibitor from the water-soluble protein fraction of wheat kernel

1989 ◽  
Vol 28 (5) ◽  
pp. 1307-1311 ◽  
Author(s):  
Elia Poerio ◽  
Lucia Carrano ◽  
Anna Maria Garzillo ◽  
Vincenzo Buonocore
Keyword(s):  
Trypsin Inhibitor ◽  
Soluble Protein ◽  
Protein Fraction ◽  
Water Soluble ◽  
Soluble Protein Fraction ◽  
Wheat Kernel ◽  
Water Soluble Protein

scholarly journals Fasciclin Domain Proteins Are Present in Nostoc Symbionts of Lichens

2002 ◽  
Vol 68 (4) ◽  
pp. 2036-2039 ◽  
Author(s):  
Per Paulsrud ◽  
Peter Lindblad
Keyword(s):  
Cell Adhesion ◽  
Soluble Protein ◽  
Protein Fraction ◽  
Open Reading Frame ◽  
Two Dimensional ◽  
Nostoc Punctiforme ◽  
Soluble Protein Fraction ◽  
Free Living ◽  
Reading Frame ◽  
Associated Proteins

ABSTRACT Differences in the soluble protein fraction between the freshly isolated cyanobiont of lichen Peltigera membranacea, the corresponding free-living strain, and Nostoc punctiforme were analyzed. One protein, which was among the most prominent proteins of the freshly isolated cyanobiont, was expressed at a lower level in the corresponding free-living strain and was not detected at all on the two-dimensional gels of N. punctiforme. This protein was partially sequenced, and the corresponding open reading frame (ORF) in the N. punctiforme genome was identified. This ORF contains a fasciclin domain typical of a class of surface-associated proteins involved in cell adhesion. Similar fasciclin motif-containing genes have previously been shown to be symbiotically induced in other symbiotic systems.

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