Ontogenetic Variation in the Multiple Hemoglobins of Arctic Charr, Salvelinus alpinus

1989 ◽  
Vol 46 (5) ◽  
pp. 804-809 ◽  
Author(s):  
M. A. Giles ◽  
D. M. Rystephanuk
Keyword(s):  
Life Cycle ◽  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Salvelinus Alpinus ◽  
Arctic Charr ◽  
Ontogenetic Variation ◽  
Starch Gel Electrophoresis ◽  
Free Swimming ◽  
Total Hemoglobin ◽  
Starch Gel

Changes during development in the multiple hemoglobins of hatchery-reared Arctic charr, Salvelinus alpinus, that originated from an anadromous stock from Nauyuk Lake, Northwest Territories were examined by starch gel electrophoresis. A total of 10 anodic and 7 cathodic hemoglobins were expressed during the life cycle of the charr. Embryos and newly-hatched alevins exhibited 10 anodic and 3 cathodic components. Of these embryonic hemoglobins, 5 anodic components and possibly 1 cathodic component with similar electrophoretic mobility were observed in older fish. In free-swimming fry 3–4 new cathodic components were expressed. Two phenotypes (designated as 3-C or 5-C) were identified in postembryonic charr, distinguished by the presence of either 3 or 5 cathodic hemoglobins, respectively. In both phenotypes the proportion of cathodic hemoglobins increased progressively with age to a maximum of 22 and 18% of total hemoglobin in the 3-C and 5-C phenotypes, respectively.

Multiple Haemoglobins of the Atlantic Salmon (Salmo salar)

1968 ◽  
Vol 25 (12) ◽  
pp. 2651-2663 ◽  
Author(s):  
N. P. Wilkins
Keyword(s):  
Life Cycle ◽  
Atlantic Salmon ◽  
Salmo Salar ◽  
Gel Electrophoresis ◽  
Initial Increase ◽  
Small Fish ◽  
Starch Gel Electrophoresis ◽  
Complete Development ◽  
Starch Gel ◽  
The Individual

The haemoglobins of over 500 salmon of different lengths, from Scotland, Greenland, and Canada have been analysed by vertical starch–gel electrophoresis at pH 8.1. Complex ontogenetic variations, involving an initial increase and later reduction in the number of fractions evident, have been observed among the anodally migrating haemoglobins. The variations observed have been correlated with changes in length, and the complete development of the anodal haemoglobin complex from the single fraction of small fish to the nine-fraction pattern of adults is outlined. The individual haemoglobin fractions appear to represent structurally distinct molecules whose regulated occurrence at different phases of the life cycle is discussed at the individual and population levels.

scholarly journals ENZYMATICALLY PRODUCED SUBUNITS OF PROTEINS FORMED BY PLASMA CELLS IN MICE

1962 ◽  
Vol 115 (3) ◽  
pp. 623-639 ◽  
Author(s):  
J. L. Fahey ◽  
Brigitte A. Askonas
Keyword(s):  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Gamma Globulin ◽  
Immunological Methods ◽  
Antigenic Determinants ◽  
Antibody Activity ◽  
Starch Gel Electrophoresis ◽  
Myeloma Protein ◽  
Γ Globulins ◽  
Starch Gel

Gamma globulin and antibody obtained from inbred C3H mice are split by papain and cysteine into fragments roughly one-third the size of the original Molecule (S20,w = 3.5S). The papain digests were characterized by starch gel electrophoresis and immunological methods. The highly heterogeneous fragments could be divided into two groups with distinct antigenic determinants (S and F), which were separated by DEAE ion-exchange cellulose chromatography. Approximately two-thirds of the fragments had S antigenic groupings and one-third had F antigenic groupings. These data are consistent with the view that mouse gamma globulin is split by papain and cysteine into three major fragments, two of which are of the S type and one of the F type. Antibody activity of the original molecule was present in the S fragments. Although the S fragments did not precipitate the antigen (hemocyanin) they were shown to bind antigen specifically in the manner of univalent antibodies. The S fragments of normal γ-globulin were very heterogeneous with a broad spectrum of electrophoretic mobilities. Comparison of S fragments from slow and fast migrating globulins showed that the mobilities of the original γ-globulin samples were largely reflected in the mobilities of their S fragments. Additional observations indicated that the F fragments also may help to determine the electrophoretic mobility of intact γ-globulin molecules. S fragments of differing electrophoretic mobility were shown to have the same antigenic determinants, indicating that the structural differences responsible for the electrophoretic mobility differences were not involved in the antigenic groupings identified with rabbit antisera. The F fragments of normal γ-globulin migrated more rapidly than the S fragments, were less heterogeneous, and showed several bands on starch gel electrophoresis. The F fragments differed antigenically from the S fragments, and had no antibody activity. Two groups of F fragments (F and F') were detected with some antisera. The γ-myeloma protein (5563) formed in a C3H plasma cell tumor and similarly fragmented by treatment with papain and cysteine, produced much more discrete S and F components than were found in the normal γ-globulin digest. The electrophoretic properties of the myeloma protein fragments were within the range observed for normal γ-globulin fragments. Although the γ-myeloma protein shares antigenic determinants with normal γ-globulins it lacks some of the antigenic groupings present in the γ-globulin preparation. Both S and F fragments from the myeloma protein share antigenic determinants with the corresponding fragments from normal γ-globulin. In addition, both S and F fragments of normal γ-globulin possess antigenic groupings not present in fragments of the γ-myeloma protein, accounting for the antigenic deficiency observed on comparison of the γ-myeloma protein with normal γ-globulins.

Ontogenetic Variation in the Multiple Hemoglobins of Coho Salmon (Oncorhynchus kisutch) and Effect of Environmental Factors on Their Expression

1976 ◽  
Vol 33 (5) ◽  
pp. 1144-1149 ◽  
Author(s):  
M. A. Giles ◽  
W. E. Vanstone
Keyword(s):  
Environmental Factors ◽  
Dissolved Oxygen ◽  
Gel Electrophoresis ◽  
Coho Salmon ◽  
Oncorhynchus Kisutch ◽  
Yolk Sac ◽  
Ontogenetic Variation ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Patterns ◽  
Starch Gel

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.

CHARACTERIZATION OF THE ESTERASES FROM ELECTRIC TISSUE OF ELECTROPHORUS BY STARCH-GEL ELECTROPHORESIS

1967 ◽  
Vol 45 (7) ◽  
pp. 1099-1105 ◽  
Author(s):  
D. J. Ecobichon ◽  
Y. Israel
Keyword(s):  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Water Soluble ◽  
Starch Gel Electrophoresis ◽  
Electrophorus Electricus ◽  
Vertical Zone ◽  
Zone Electrophoresis ◽  
Starch Gel

The water-soluble esterases of a microsome-free supernatant of the electric tissue of Electrophorus electricus were separated by vertical-zone electrophoresis in starch gel. Specific and nonspecific substrates and inhibitors were used in conjunction with histochemical techniques to identify the enzymes. Acetylcholinesterase was present in the form of four bands of activity, the electrophoretic mobility of which was suggestive of aggregated forms of the enzyme. Pseudocholinesterase was detected as two weak bands of activity. A third esterase was identified as a nonspecific carboxylesterase and shown to be a sialoprotein.

Isolation of κ-casein-like fractions from human whole casein by chromatography on thiol-Sepharose, hydroxyapatite and DEAE-cellulose

1981 ◽  
Vol 48 (3) ◽  
pp. 429-436 ◽  
Author(s):  
Jean-Marc Chobert ◽  
Francesco Addeo ◽  
Bruno Ribadeau Dumas
Keyword(s):  
Affinity Chromatography ◽  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Phosphate Buffer ◽  
Deae Cellulose ◽  
The Other ◽  
Starch Gel Electrophoresis ◽  
Sh Groups ◽  
Starch Gel

SummaryDifferent fractions of human κ-casein characterized by their sensitivity to chymosin were separated, after reduction, by affinity chromatography on thiol-Sepharose in a 0·1 m-Tris-HCl buffer, pH 7·0, containing 7 M-urea, 0·3 m-NaCl and 1 mm-EDTA. The fraction retained on the column and bearing the SH-groups was then chromatographed on hydroxyapatite in a 5 mm-phosphate buffer, pH 6·8, containing 0·2 m-KC1, 4·5 m-urea and 2 mm 2-mercaptoethanol. The fraction not retained on this column was purified by chromatography on DEAE-cellulose in a 6·6 m-urea, 0·02 m-imidazole, 0·02 m 2-mercaptoethanol buffer, pH 7·0. Two chymosinsensitive fractions were identified by starch-gel electrophoresis at pH 8·6; one of low electrophoretic mobility, the other a smeared band covering the whole distance of migration, in which several bands with mobilities greater than those of β-caseins could be detected.

CHANGES IN THE MULTIPLE HEMOGLOBIN PATTERNS OF SOME PACIFIC SALMON, GENUS ONCORHYNCHUS, DURING THE PARR–SMOLT TRANSFORMATION

1964 ◽  
Vol 42 (6) ◽  
pp. 697-703 ◽  
Author(s):  
W. E. Vanstone ◽  
Eve Roberts ◽  
H. Tsuyuki
Keyword(s):  
Life Cycle ◽  
Gel Electrophoresis ◽  
Sockeye Salmon ◽  
Coho Salmon ◽  
Pacific Salmon ◽  
Starch Gel Electrophoresis ◽  
Mature Adults ◽  
Salmon Fry ◽  
Starch Gel ◽  
Sexually Mature

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.

Fractionation of Plasminogen by Starch Gel Electrophoresis

1964 ◽  
Vol 12 (01) ◽  
pp. 126-136 ◽  
Author(s):  
Karl H. Slotta ◽  
J. D Gonzalez
Keyword(s):  
Gel Electrophoresis ◽  
Room Temperature ◽  
Broad Band ◽  
Caproic Acid ◽  
Starch Gel Electrophoresis ◽  
Full Activity ◽  
Veronal Buffer ◽  
Starch Gel ◽  
Alkaline Range

SummaryWhen urea or ε-amino caproic acid were used as solublizing agents for plasminogen in electrophoretic experiments, only one broad band of the proenzyme was obtained on acetate cellulose, in starch block, and in acrylamide gel. In starch gel electrophoresis, however, both forms of plasminogen – the native or euglobulin and Kline’s or Pseudoglobulin plasminogen – separated into six bands. These migrated toward the cathode at room temperature in borate or veronal buffer in the alkaline range and showed full activity in fibrinagar-streptokinase plates.

scholarly journals THE INHERITANCE OF ENZYME VARIANTS FOR TYROSINE AMINOTRANSFERASE, NADP-DEPENDENT MALATE DEHYDROGENASE, NADP-DEPENDENT ISOCITRATE DEHYDROGENASE, AND TETRAZOLIUM OXIDASE IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt
Keyword(s):  
Detailed Analysis ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Tyrosine Aminotransferase ◽  
Breeding Program ◽  
Starch Gel Electrophoresis ◽  
Enzyme Locus ◽  
Starch Gel

ABSTRACT The isozymic patterns of tyrosine aminotransferase, NADP malate dehydrogenase, NADP isocitrate dehydrogenase, and tetrazolium oxidase were examined by starch-gel electrophoresis in Tetrahymena pyriformis, syngen 1. The genetics of the alleles controlling these enzymes was studied through a breeding program. Each enzyme locus was shown to assort vegetatively, as do other loci in this organism. A detailed analysis of the assortment process for the tyrosine aminotransferase locus indicated that the rate of stabilization of heterozygotes into pure types was essentially identical to previously-reported rates for other loci.

Sign in / Sign up

Export Citation Format

Share Document