Specific Binding of the Syringolide Elicitors to a Soluble Protein Fraction from Soybean Leaves

1997 ◽  
Vol 9 (8) ◽  
pp. 1425
Author(s):  
Cheng Ji ◽  
Yasushi Okinaka ◽  
Yoji Takeuchi ◽  
Tetsu Tsurushima ◽  
Richard I. Buzzell ◽  
...  
Keyword(s):  
Soluble Protein ◽  
Protein Fraction ◽  
Specific Binding ◽  
Soluble Protein Fraction ◽  
Soybean Leaves

scholarly journals Specific Binding of the Syringolide Elicitors to a Soluble Protein Fraction from Soybean Leaves.

1997 ◽  
pp. 1425-1433 ◽  
Author(s):  
C. Ji ◽  
Y. Okinaka ◽  
Y. Takeuchi ◽  
T. Tsurushima ◽  
R. I. Buzzell ◽  
...  
Keyword(s):  
Soluble Protein ◽  
Protein Fraction ◽  
Specific Binding ◽  
Soluble Protein Fraction ◽  
Soybean Leaves

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.

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 Effects of HSPA8, an evolutionarily conserved oviductal protein, on boar and bull spermatozoa

Reproduction ◽  
2009 ◽  
Vol 137 (2) ◽  
pp. 191-203 ◽  
Author(s):  
Roslyn M A Elliott ◽  
Rhiannon E Lloyd ◽  
Alireza Fazeli ◽  
Edita Sostaric ◽  
A Stephen Georgiou ◽  
...  
Keyword(s):  
Soluble Protein ◽  
Protein Fraction ◽  
Mammalian Species ◽  
Surface Proteins ◽  
Apical Plasma Membrane ◽  
Enhancement Effect ◽  
Soluble Protein Fraction ◽  
Sperm Survival ◽  
Pre Treatment

Previous studies have shown that a soluble protein fraction derived from preparations of apical plasma membrane (APM) of the oviductal epithelium enhances the in vitro survival of mammalian spermatozoa. Here, we show that the survival enhancing property of the soluble protein fraction seems to depend significantly upon heat shock 70 kDa protein 8 (HSPA8 previously known as HSPA10). The following findings in the present study enabled us to draw this conclusion: first, using proteomic analysis, we identified a subset of 70 kDa oviductal surface proteins that bound to spermatozoa, one of which was HSPA8. Second, pre-treatment of the soluble protein fraction with anti-HSPA8 antibody reduced the 24 h (at 39 °C) sperm survival enhancement effect normally induced by the presence of 200 μg/ml soluble APM proteins. Third, complementary experiments showed that substituting the soluble protein fraction with bovine recombinant HSPA8 (0.5–2 μg/ml) also elicited the sperm survival effect. Finally, we also tested the effect of bovine recombinant HSPA8 on bull spermatozoa and found similar, dose-responsive, sperm survival promoting effects. The conserved nature of HSPA8 between mammalian species suggests that this protein may represent a common biological mechanism for the maintenance of sperm survival in the oviduct.

scholarly journals Ca2+-dependent binding of cytosolic components to insulin-secretory granules results in Ca2+-dependent protein phosphorylation

1983 ◽  
Vol 210 (2) ◽  
pp. 533-539 ◽  
Author(s):  
K W Brocklehurst ◽  
J C Hutton
Keyword(s):  
Protein Phosphorylation ◽  
Soluble Protein ◽  
Protein Fraction ◽  
Islet Cell ◽  
Secretory Granules ◽  
Dependent Manner ◽  
Soluble Protein Fraction ◽  
Islet Cell Tumour ◽  
Insulin Granules ◽  
Dependent Protein

1. Incubation of a rat islet cell tumour homogenate with [gamma-32P]ATP resulted in the Ca2+-dependent phosphorylation of 100000-, 57000-, 29000-, 26000- and 14000-Mr proteins. The Ca2+ concentration required was in the low-microM range. 2. Isolated insulin granules did not exhibit Ca2+-dependent protein phosphorylation, whereas a soluble protein fraction showed the Ca2+-dependent phosphorylation of a 57000-Mr protein. Combination of insulin granules with the soluble protein fraction resulted in the additional Ca2+-dependent phosphorylations of 100000-, 29000- and 10000-Mr proteins. The latter phosphorylations were not enhanced by exogenous calmodulin, but nevertheless were inhibited by trifluoperazine. Removal of endogenous calmodulin from the soluble protein fraction before incubation with insulin granules did not abolish the Ca2+-dependent phosphorylations of the 100000-, 29000- and 10000-Mr proteins but rendered the Ca2+-dependent phosphorylation of the 57000-Mr soluble protein dependent on exogenous calmodulin. 3. The components of the soluble protein fraction responsible for the interaction with insulin granules bound to intact granules in a Ca2+-dependent manner. 4. After phosphorylation, the 29000-Mr protein remained attached to granules, whereas the 100000- and 10000-Mr proteins dissociated from granules. 5. These Ca2+-dependent phenomena may be of regulatory importance in the secretory mechanism.

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