Starch-gel electrophoresis of malate dehydrogenase

Author(s):  
C.J.R. Thorne ◽  
L.I. Grossman ◽  
N.O. Kaplan
Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt

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.


1974 ◽  
Vol 31 (3) ◽  
pp. 342-345 ◽  
Author(s):  
J. W. Clayton ◽  
R. E. K. Harris ◽  
D. N. Tretiak

Walleye (Stizostedion vitreum vitreum) populations from western Canada contain three alleles for supernatant malate dehydrogenase (MDH). The protein subunits specified by these alleles produce isozymes that are readily distinguished by starch gel electrophoresis procedures. One of the MDH alleles (c1) appears to reach a maximum frequency of about 0.6 in the walleye populations of Crean and Montreal lakes, two headwater lakes in central Saskatchewan. The frequency of this allele declines to about 0.1 in populations only a relatively short distance downstream from these headwater lakes. In most walleye populations tested the c2 and c3 alleles predominate at frequencies between 0.2 and 0.7, whereas c1 is usually comparatively rare and occurs at a frequency of about 0.05.


Bragantia ◽  
1999 ◽  
Vol 58 (1) ◽  
pp. 01-06 ◽  
Author(s):  
ADILSON RICKEN SCHUELTER ◽  
VICENTE WAGNER DIAS CASALI ◽  
FERNANDO LUIZ FINGER

Leaf extracts from wild pepper (Capsicum flexuosum Sendt) were analysed for the presence of malate dehydrogenase (E.C. 1.1.1.37; MDH) isozymes using starch gel electrophoresis. Seven phenotypes for MDH isozymes were observed in the genitors. Genetic analysis in F1 progenies revealed five loci coding for MDH. Isozyme banding patterns of hybrids indicated that MDH-3 and MDH-4 genes code for monomeric enzymes, while MDH-5 for a dimeric isoform. In MDH-2 loci, one particular F1 progeny showed a significant deviation from the expected isozyme pattern. It is possible that other genes are controlling the expression of MDH-2 in pepper. Also, there are two alleles coding for MDH-2 isozyme. On the other hand, MDH-1 was monomorphic for all genotypes used in the experiment.


1964 ◽  
Vol 12 (01) ◽  
pp. 126-136 ◽  
Author(s):  
Karl H. Slotta ◽  
J. D Gonzalez

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.


1963 ◽  
Vol 41 (1) ◽  
pp. 369-387 ◽  
Author(s):  
J. M. Neelin

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.


1981 ◽  
Vol 59 (5) ◽  
pp. 771-775 ◽  
Author(s):  
Moira M. Ferguson ◽  
David L. G. Noakes ◽  
Roy G. Danzmann

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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