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.

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.

Species Differences of Some Members of Salmonidae Based on Their Muscle Myogen Patterns

1963 ◽  
Vol 20 (1) ◽  
pp. 101-104 ◽  
Author(s):  
H. Tsuyuki ◽  
E. Roberts
Keyword(s):  
Atlantic Salmon ◽  
Gel Electrophoresis ◽  
Brook Trout ◽  
Species Differences ◽  
Pink Salmon ◽  
Starch Gel Electrophoresis ◽  
Protein Patterns ◽  
Dolly Varden ◽  
Constant Property ◽  
Starch Gel

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.

scholarly journals Die Trennung der Hämolymphe-Proteine bei Vorpuppen und Puppen der Galleria mellonella L. mittels Gel-Filtration auf Sephadex G-200, Bestimmung ihrer isoelektrischen Punkte und ihrer Molekulargewichte / Separation of Haemolymph Proteins of Prepuae and Pupae of Galleria mellonella L. by means of Gel Filtration on Sephadex 200, Determination of their Isoelectric Points and their Molecular Weights

1969 ◽  
Vol 24 (6) ◽  
pp. 732-740 ◽  
Author(s):  
Milan Marek
Keyword(s):  
Gel Electrophoresis ◽  
Galleria Mellonella ◽  
Gel Filtration ◽  
Starch Gel Electrophoresis ◽  
Molecular Weights ◽  
Isoelectric Points ◽  
Starch Gel ◽  
The Individual ◽  
Naphthyl Acetate

Gel filtration on Sephadex G-200 was carried out on haemolymph proteins of prepupae. ligatured prepupae, male and female pupae and cooled pupae of Galleria mellonella L.The proteins were separated into two main fractions. The esterase activity of the eluated haemolymph was determined by means of beta-naphthyl acetate after filtration.After elution the samples were condensed and additionally separated on horizontal starch-gel electrophoresis.The “cooling protein” of pupae and the “ligature protein” of ligatured larvae of Galleria mellonella were shown by means of starch-gel electrophoresis to be new proteins, so far not described.The isoelectric point and molecular weight were determined for the individual protein fractions.They were then stained with amido black 10 B for the proof of proteins, and with alpha-naphthyl butyrate with Fast-Blue BB salt for the identification of esterases.

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.

STARCH GEL ELECTROPHORESIS OF MYOGEN FROM CHICKEN BREAST MUSCLE IN CONSTANT AND GRADIENT BUFFER SYSTEMS

1963 ◽  
Vol 41 (1) ◽  
pp. 369-387 ◽  
Author(s):  
J. M. Neelin
Keyword(s):  
Gel Electrophoresis ◽  
Protein Concentration ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Starch Gel Electrophoresis ◽  
Two Dimensional ◽  
Sodium Cacodylate ◽  
Gradient Systems ◽  
Optimal Separation ◽  
Starch Gel

By varying conditions of starch gel electrophoresis, factors contributing to the resolution of myogen proteins from chicken breast muscle have been studied. Variables examined included composition of the myogen extractant, protein concentration, ionic strength of electrophoretic media, pH of gel media, plane and direction of electrophoresis, and the nature of cations and anions in gel media and bridge solutions. The significance of anions was more closely studied with constant buffer systems, and gradient systems in which bridge electrolyte differed from, and gradually altered, the gel medium. Optimal separation was obtained in gradient systems with 0.10 M sodium chloride bridge solutions, and gel media of sodium cacodylate, pH 6.9, μ 0.010, which resolved 12 cationic zones, and sodium veronal, pH 7.4, μ 0.010, which resolved 10 anionic zones. These buffers in two-dimensional sequence revealed a total of about 24 components in this myogen.

Morphological and biochemical systematics of chubs, Nocomis biguttatus and N. micropogon (Pisces: Cyprinidae), in southern Ontario

1981 ◽  
Vol 59 (5) ◽  
pp. 771-775 ◽  
Author(s):  
Moira M. Ferguson ◽  
David L. G. Noakes ◽  
Roy G. Danzmann
Keyword(s):  
Gel Electrophoresis ◽  
Function Analysis ◽  
Morphological Differentiation ◽  
Sexually Dimorphic ◽  
Starch Gel Electrophoresis ◽  
Southern Ontario ◽  
Electrophoretic Mobilities ◽  
Starch Gel ◽  
Respective Species ◽  
Probability Of Misclassification

Examination of 17 presumptive gene loci by starch-gel electrophoresis revealed differential mobilities only at acid phosphatase-1, alcohol dehydrogenase, esterase-1, and phosphoglucomutase between Nocomis biguttatus and N. micropogon. No intraspecific variation was observed for any loci. The genetic identity (I) and genetic distance (D) were 0.874 and 0.134, respectively. The correlation of electrophoretic mobilities and nuptial tubercle pattern in sexually dimorphic males supports the present taxonomic distinction of these species and provides a simple, unambiguous means of identifying any individuals.Stepwise discriminant function analysis of a series of mensural characters was used to compare fish identified as to species by electrophoresis. At best this correctly assigned fish to their respective species in 85.7% of cases, with a probability of misclassification of 0.1335.This study suggests these two are sibling species, based on a comparison of biochemical and morphological differentiation.

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