MUSCLE PROTEINS OF PACIFIC SALMON (ONCORHYNCHUS): III. THE SEPARATION OF MUSCLE PROTEINS SOLUBLE IN LOW IONIC STRENGTH SALT SOLUTIONS BY STARCH GEL ELECTROPHORESIS

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.

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.


1964 ◽  
Vol 42 (6) ◽  
pp. 697-703 ◽  
Author(s):  
W. E. Vanstone ◽  
Eve Roberts ◽  
H. Tsuyuki

By employing starch gel electrophoresis it has been found that coho salmon fry and smolts contain 10 anodal-migrating, and 12 cathodal-migrating, hemoglobin fractions. Prepuberal [Formula: see text]-year-old coho salmon caught at sea and sexually mature adults taken from fresh water contained the same anodal fractions and at approximately the same concentrations as were found in fry and smolts. However, the concentrations of the cathodal fractions had increased so that these were very nearly equal to those of the anodal fractions. Similar hemoglobin changes were found in both anadromous and land-locked sockeye salmon, but in this species seven anodal and six cathodal fractions were present at their "adult" concentrations in fry and smolts. Six other cathodal fractions which were absent entirely or present only in trace amounts in fry and smolts increased to their adult concentrations some time later in the life cycle of both varieties of sockeye. It is postulated that these changes reflect an ecological adaption to life in the ocean.


1962 ◽  
Vol 40 (7) ◽  
pp. 919-927 ◽  
Author(s):  
H. Tsuyuki ◽  
E. Roberts ◽  
R. E. A. Gadd

The muscle myogens and other components of the spring salmon (O. tshawytscha), chum salmon (O. keta), coho salmon (O. kisutch), and sockeye salmon (O. nerka), as well as the lingcod (Ophiodon elongatus), were separated by the use of diethylaminoethyl (DEAE) cellulose columns. Significant amounts of slowly dialyzable inosine and inosinic acid which may lead to spurious peaks in moving-boundary electrophoretic separations have been shown to be present in the muscle myogen preparations. The basic differences in the muscle myogen components of the Pacific salmon and the lingcod are compared.


1966 ◽  
Vol 44 (10) ◽  
pp. 1357-1364 ◽  
Author(s):  
Shun-Fong Hui ◽  
R. H. Common

Starch-gel electrophoresis of the total livetins of hen's egg yolk resolved 16 zones: seven major zones, six minor zones, and three faint, diffuse zones. One zone was identified with the major component of paper electrophoretic alpha-livetin and hence with serum albumin. Four of the major zones were identified with the major components of paper electrophoretic beta-livetin on the one hand, and with an electrophoretically heterogeneous livetin antigen (livetin antigen 3) on the other hand, thus establishing the electrophoretic heterogeneity and relative immunological homogeneity of the paper electrophoretic beta-livetin fraction. The other two major starch-gel electrophoretic zones were identified as transferrins by their positive staining reaction for iron and comparison of their mobilities with two corresponding serum starch-gel fractions.


1976 ◽  
Vol 33 (5) ◽  
pp. 1144-1149 ◽  
Author(s):  
M. A. Giles ◽  
W. E. Vanstone

Hemolyzates from the blood of coho salmon (Oncorhynchus kisutch) at various stages of development were subjected to micro-starch-gel electrophoresis. Three distinct electrophoretic patterns composed of different combinations of 18 hemoglobin tetramers were observed. Embryonic and yolk-sac alevins possessed 1 cathodic and 12 anodic components while fry retained only 3 of the 12 anodic polymorphs. During smoltification, 4 new cathodic components appeared and 2 of the anodic and the cathodic components of alevin hemolyzates reappeared. This latter pattern was retained until the fish spawned and died. Attempts to induce changes in the pattern of development of these hemoglobins by exposing fry and pre-smolts to extreme variations in dissolved oxygen, temperature, and salinity were completely unsuccessful.


1963 ◽  
Vol 20 (1) ◽  
pp. 101-104 ◽  
Author(s):  
H. Tsuyuki ◽  
E. Roberts

The muscle myogen patterns obtained by starch gel electrophoresis of the Dolly Varden and eastern brook trout (Salvelinus), the rainbow and steelhead trouts and the Atlantic salmon (Salmo), and the coho, spring, chum, sockeye and pink salmon (Oncorhynchus) are compared. The myogen protein patterns are clearly distinct for each species of fishes studied, except for the rainbow and steelhead trouts, and constitute a remarkably constant property which can be employed to differentiate between species and for other useful purposes. The specific and generic inter-relationships have been analyzed by these patterns and developed as further criteria for classification purposes and are discussed in conjunction with currently accepted beliefs.


1962 ◽  
Vol 40 (1) ◽  
pp. 919-927 ◽  
Author(s):  
H. Tsuyuki ◽  
E. Roberts ◽  
R. E. A. Gadd

The muscle myogens and other components of the spring salmon (O. tshawytscha), chum salmon (O. keta), coho salmon (O. kisutch), and sockeye salmon (O. nerka), as well as the lingcod (Ophiodon elongatus), were separated by the use of diethylaminoethyl (DEAE) cellulose columns. Significant amounts of slowly dialyzable inosine and inosinic acid which may lead to spurious peaks in moving-boundary electrophoretic separations have been shown to be present in the muscle myogen preparations. The basic differences in the muscle myogen components of the Pacific salmon and the lingcod are compared.


1968 ◽  
Vol 107 (2) ◽  
pp. 139-150 ◽  
Author(s):  
R. K. Scopes

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.


1964 ◽  
Vol 10 (1) ◽  
pp. 62-68 ◽  
Author(s):  
Tatsuo Hase

Abstract A simple microelectrophoretic method of protein analysis using the gel of starch agar mixture is described. The method is easily standardized and the results show consistency and reproducibility. Protein patterns obtained show higher resolution than those of paper or agar-gel electrophoresis and simulate that of starch-gel electrophoresis. Developed protein patterns are suitable to quantitative analysis by appropriate electrophotometric or ultraviolet-light scanning devices and can be preserved as permanent records.


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