The relationship between nematodes of the genus Cosmocercoides Wilkie, 1930 (Nematoda: Cosmocercoidea) in toads (Bufo americanus) and slugs (Deroceras laeve)

1987 ◽  
Vol 65 (7) ◽  
pp. 1650-1661 ◽  
Author(s):  
Daryl J. Vanderburgh ◽  
R. C. Anderson
Keyword(s):  
Discriminant Analysis ◽  
Gel Electrophoresis ◽  
Analysis Of Covariance ◽  
Starch Gel Electrophoresis ◽  
Bufo Americanus ◽  
Cross Transmission ◽  
Starch Gel ◽  
The Relationship

Nematodes of the genus Cosmocercoides Wilkie, 1930 from Bufo americanus and Deroceras laeve, generally considered to belong to the same species (Cosmocercoides dukae), were compared. Male worms from B. americanus had 20 or 21 rosette papillae per subventral row whereas males from D. laeve had 13 to 14. Worms from toads had numerous simple postanal papillae. Worms from slugs generally lacked such papillae. Worms from the two hosts differed morphometrically and were well separated by discriminant analysis after bias of worm length was removed by analysis of covariance. Differences in isoenzyme migration were detected using starch gel electrophoresis. In cross-transmission experiments, more toads became infected when exposed to larvae of worms from toads than when exposed to larvae of worms from slugs. More slugs became infected when exposed to larvae from slugs than when exposed to larvae from toads. Intensity of mature worms recovered was significantly (p < 0.05) greater (and patent infections developed) when transmission was from toad to toad or from slug to slug than when transmission was from toad to slug or from slug to toad. No patent infections were recorded from toads or slugs exposed to larvae from the unrelated host. The results indicate that worms in toads and slugs are not conspecific. Cosmocercoides variabilis (Harwood, 1930) Travassos, 1931 is resurrected as the name of the species occurring in B. americanus, Cosmoceroides dukae (Holl, 1928) Travassos, 1931 is retained as the name of the species occurring in D. laeve.

scholarly journals The relationship between reversibility of fibril formation and subunit composition of rat skin collagen

1969 ◽  
Vol 113 (2) ◽  
pp. 419-422 ◽  
Author(s):  
D. W. Bannister
Keyword(s):  
Acetic Acid ◽  
Gel Electrophoresis ◽  
Fibril Formation ◽  
Subunit Composition ◽  
Starch Gel Electrophoresis ◽  
Rat Skin ◽  
Fractionation Procedure ◽  
Skin Collagen ◽  
Starch Gel ◽  
The Relationship

1. Salt-soluble rat skin collagen was precipitated from solution at neutral pH and 37°. On cooling, a portion of the collagen returned into solution. The fractions were separated, the supernatant was concentrated and the precipitate was redissolved in dilute acetic acid. 2. Solutions of supernatant and precipitate were subjected to the same fractionation procedure, giving four fractions. 3. Each fraction was examined by starch-gel electrophoresis and a relationship between subunit composition and the fractionation procedure was noted. The collagen that redissolved on cooling contained less of the more highly cross-linked components than did either the fraction remaining in the precipitate or the starting material.

scholarly journals The nature of the multiple forms of cytoplasmic aspartate aminotransferase from pig and sheep heart

1974 ◽  
Vol 141 (2) ◽  
pp. 401-406 ◽  
Author(s):  
Robert John ◽  
Richard Jones
Keyword(s):  
Aspartate Aminotransferase ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Wide Range ◽  
Covalent Structure ◽  
Starch Gel ◽  
The Difference ◽  
Ph Range ◽  
The Relationship ◽  
Charged Group

Starch-gel electrophoresis of sheep heart aspartate aminotransferase was carried out over the range pH7.0–8.5. The enzyme separates into three subforms in the same way as the pig heart enzyme. As the pH was increased the distance migrated by each subform increased by the same amount, so that they remained the same distance apart. Titration of the enzyme over the appropriate pH range was used to calculate the difference in charge between the subforms and it was concluded that they differ by one charged group per dimer from their nearest neighbour on the electrophoretogram over the whole pH range studied. It was also shown that the pig-heart α and β subforms differ by almost one charged group per dimer in the range pH5.5–5.7 and that the spacing between the subforms on starch-gel electrophoresis at pH8.0 is the same as that for the sheep enzyme. Since the charge difference between the subforms is maintained over such a wide range of pH, it is concluded that they probably differ from each other in covalent structure, because of the improbability that conformational differences can give rise to such behaviour. The relationship between the subforms and inactive binding of the coenzyme is also examined.

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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