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.

Comparative zone electrophoresis of catalase of Staphylococcus species isolated from mammalian skin

1976 ◽  
Vol 22 (12) ◽  
pp. 1691-1698 ◽  
Author(s):  
Raymond J. Zimmerman
Keyword(s):  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Polyacrylamide Electrophoresis ◽  
Electrophoretic Mobilities ◽  
Mammalian Skin ◽  
Zone Electrophoresis ◽  
Starch Gel ◽  
Molecular Sieving

Vertical polyacrylamide slab gel electrophoresis was conducted for the catalase enzymes of representative strains of 18 proposed species and subspecies of the genus Staphylococcus. The catalase bands which resulted were predominantly monomorphic within each of the species and differences in catalase mobilities were observed between many of the species. The electrophoretic mobilities of the catalases were supportive to the scheme of classification used. Many strains of certain species demonstrated multiple catalase bands which are suggestive of multimolecular forms of the enzyme. Horizontal starch gel electrophoresis of representative strains of S. capitis produced catalase bands with relative mobilities that were different from those obtained with polyacrylamide electrophoresis, presumably due to a difference in molecular sieving between the gels.

STUDIES ON HUMAN CHORIONIC GONADOTROPHIN

1968 ◽  
Vol 59 (1) ◽  
pp. 120-138 ◽  
Author(s):  
A. H. W. M. Schuurs ◽  
E. de Jager ◽  
J. D. H. Homan
Keyword(s):  
Gel Electrophoresis ◽  
Complement Fixation ◽  
Haemagglutination Inhibition ◽  
Fundamental Difference ◽  
Chorionic Gonadotrophin ◽  
Human Chorionic Gonadotrophin ◽  
Starch Gel Electrophoresis ◽  
International Standard ◽  
Electrophoretic Mobilities ◽  
Starch Gel

ABSTRACT Preparations of Human Chorionic Gonadotrophin (HCG) with varying degrees of homogeneity were investigated immunochemically. The preparations were compared qualitatively by combined starch gel electrophoresis and immunoelectrophoresis, by immunodiffusion and immunoelectrophoresis in agar, and, quantitatively by haemagglutination inhibition and by complement fixation reactions. The components present in pure HCG preparations which differed in electrophoretic mobilities, in N-acetyl neuraminic acid (NANA) content and in biological potencies, appeared to be immunochemically identical. This implies that results of immunochemical and biological estimations need not correlate with each other. This finding is compared with relevant data in the literature. It is proposed to use the 2nd International Standard for HCG for both immunochemical and biological estimations, but, because of the fundamental difference between the results of the two types of estimations, to express the immunochemically determined values in »International Immunochemical Units« (IIU).

scholarly journals LINKAGE ANALYSIS OF THE MULTILOCUS GLUCOSEPHOSPHATE ISOMERASE ISOZYME SYSTEM IN SUNFISH (CENTRARCHIDAE, TELEOSTII)

Genetics ◽  
1976 ◽  
Vol 82 (1) ◽  
pp. 35-42
Author(s):  
Gregory S Whitt ◽  
William F Childers ◽  
James B Shaklee ◽  
Janet Matsumoto
Keyword(s):  
High Frequency ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Glucosephosphate Isomerase ◽  
Electrophoretic Mobilities ◽  
Starch Gel ◽  
Allelic Isozymes ◽  
F2 Generation ◽  
Species Specific ◽  
Green Sunfish

ABSTRACT The purpose of the present investigation is to determine whether the two duplicated glucosephosphate isomerase (EC 5.3.1.9) loci Gpi-A and Gpi-B reside on the same chromosome in teleostean fishes. Interspecific sunfish hybrids were employed for the cross because of the different species-specific electrophoretic mobilities of the allelic isozymes at each GPI locus and because of their genomic compatibility. F1 sunfish hybrids, formed from a male warmouth (Lepomis gulosus) × female green sunfish (L. cyanellus) cross, were mated to form the F2 generation. The number of each of the nine different isozyme phenotypes, revealed by starch gel electrophoresis, was determined using 256 F2 individuals. The high frequency of recombinant phenotypes in the F2 generation indicated that the two GPI loci are not linked. An excess of F2 individuals heterozygous at both loci was observed and is interpreted as being caused by heterosis. The absence of linkage for the homologous loci encoding GPI subunits and for other multilocus isozyme systems is consistent with the postulate that the genomes of present-day vertebrates arose through one or more polyploidization events early in vertebrate evolution.

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.

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