Muscle Proteins of Pacific Salmon (Oncorhynchus): I. A Note on the Separation of Muscle Proteins Soluble in Low Ionic Strength Salt Solutions

1961 ◽  
Vol 18 (4) ◽  
pp. 637-640 ◽  
Author(s):  
H. Tsuyuki ◽  
Eve Roberts

not available




1962 ◽  
Vol 40 (7) ◽  
pp. 929-936 ◽  
Author(s):  
H. Tsuyuki ◽  
E. Roberts ◽  
R. E. A. Gadd

By the use of starch gel electrophoretic technique the muscle myogens of the five Pacific west coast species of the Oncorhynchus genus, the steelhead trout (representative of the genus Salmo), the lingcod, and Atlantic cod have been separated. The characteristic protein patterns were used to group the members of the Oncorhynchus genus into sockeye, pink, and chum salmon on the one hand and the spring and coho salmon on the other. Correlation of the groupings based upon their protein pattern is discussed in relation to a similar grouping arrived at through behavior studies by other workers. The relationship between column and gel electrophoretic separations has been investigated.



Author(s):  
D. Rittschof ◽  
C.M. Kratt ◽  
A.S. Clare

Gastropod shells are essential to most hermit crabs. Shell availability limits hermit crab populations. Shells provide protection and the degree of shell-fit controls crab growth and fecundity. Crabs locate new gastropod shells from a distance under water by molecules released from gastropod flesh during predation events. Here we test the hypothesis that the salivary glands of the predatory gastropod are the source of enzymes that digest muscle proteins and release peptide attractants. We describe the anatomy of both the acinous salivary glands and the tubular accessory salivary glands of Busycon contrarium which are similar to those of B. carica. The salivary gland ducts empty at the mouth, suggesting a role in the primary digestion of food. We show that gastropod muscle proteins, extracted by salt solutions with the ionic strength of sea water and purified by precipitation in low ionic strength can be digested by gastropod salivary gland enzymes to generate peptides attractive to the hermit crab, Clibanarius vittatus, in field assays.



1996 ◽  
Vol 44 (2) ◽  
pp. 408-415 ◽  
Author(s):  
Ganesan Krishnamurthy ◽  
Hsin-Sui Chang ◽  
Herbert O. Hultin ◽  
Yuming Feng ◽  
Subramanian Srinivasan ◽  
...  


1962 ◽  
Vol 40 (1) ◽  
pp. 929-936 ◽  
Author(s):  
H. Tsuyuki ◽  
E. Roberts ◽  
R. E. A. Gadd

By the use of starch gel electrophoretic technique the muscle myogens of the five Pacific west coast species of the Oncorhynchus genus, the steelhead trout (representative of the genus Salmo), the lingcod, and Atlantic cod have been separated. The characteristic protein patterns were used to group the members of the Oncorhynchus genus into sockeye, pink, and chum salmon on the one hand and the spring and coho salmon on the other. Correlation of the groupings based upon their protein pattern is discussed in relation to a similar grouping arrived at through behavior studies by other workers. The relationship between column and gel electrophoretic separations has been investigated.



2012 ◽  
Vol 101 (3) ◽  
pp. 965-977 ◽  
Author(s):  
Le Zhang ◽  
Helming Tan ◽  
R. Matthew Fesinmeyer ◽  
Cynthia Li ◽  
David Catrone ◽  
...  


1980 ◽  
Vol 41 (1) ◽  
pp. 135-149
Author(s):  
D. Gingell ◽  
I. Todd

Using both living and glutaraldehyde-fixed red cells, we have examined adhesion to both oil/saline and glass/saline interfaces by interference reflection microscopy. At low ionic strength, 0.4 mM NaCl, fixed cells adherent to the oil/saline interface show first order whitish yellow zones of closest approach which indicate a separation of similar to or approximately 100 nm. Quantitative interferometry in monochromatic light supports this conclusion. As the salt concentration is increased the separation decreases and the final image shows zero-order black which probably indicates molecular contact with the interface. Similar but less reproducible results were obtained with fixed and unfixed cells on glass. Thes observations show that physical interactions alone can be responsible for adhesion in dilute and concentrated salt solutions. It is not, however, believed that the results necessarily imply the existence of adhesion with a gap in physiological concentrations of salt.





Author(s):  
J.S. Wall ◽  
V. Maridiyan ◽  
S. Tumminia ◽  
J. Hairifeld ◽  
M. Boublik

The high contrast in the dark-field mode of dedicated STEM, specimen deposition by the wet film technique and low radiation dose (1 e/Å2) at -160°C make it possible to obtain high resolution images of unstained freeze-dried macromolecules with minimal structural distortion. Since the image intensity is directly related to the local projected mass of the specimen it became feasible to determine the molecular mass and mass distribution within individual macromolecules and from these data to calculate the linear density (M/L) and the radii of gyration.2 This parameter (RQ), reflecting the three-dimensional structure of the macromolecular particles in solution, has been applied to monitor the conformational transitions in E. coli 16S and 23S ribosomal RNAs in solutions of various ionic strength.In spite of the differences in mass (550 kD and 1050 kD, respectively), both 16S and 23S RNA appear equally sensitive to changes in buffer conditions. In deionized water or conditions of extremely low ionic strength both appear as filamentous structures (Fig. la and 2a, respectively) possessing a major backbone with protruding branches which are more frequent and more complex in 23S RNA (Fig. 2a).



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