scholarly journals ON THE IDENTITY OF "NOTHING DEHYDROGENASE"

1965 ◽  
Vol 13 (6) ◽  
pp. 431-433 ◽  
Author(s):  
CHARLES R. SHAW ◽  
ANN L. KOEN
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Gel Electrophoresis ◽  
Histochemical Demonstration ◽  
Starch Gel Electrophoresis ◽  
Quantitative Measurements ◽  
Pure Alcohol ◽  
Mouse Tissues ◽  
Starch Gel

The histochemical demonstration of dehydrogenase activity using tetrazolium sometimes occurs in the absence of added substrate. This occurrence has been called "nothing dehydrogenase". The present study, based on starch gel electrophoresis of mouse tissues and of pure alcohol dehydrogenase, as well as quantitative measurements of the latter, indicates that alcohol dehydrogenase is the major agent of "nothing dehydrogenase" activity.

scholarly journals Identifying Crabapple Cultivars by Isozymes

1995 ◽  
Vol 120 (5) ◽  
pp. 706-709 ◽  
Author(s):  
Robert D. Marquard ◽  
Charlotte R. Chan
Keyword(s):  
Alcohol Dehydrogenase ◽  
Gel Electrophoresis ◽  
Cultivar Identification ◽  
Enzyme System ◽  
Starch Gel Electrophoresis ◽  
Shikimate Dehydrogenase ◽  
Polymorphic Region ◽  
Banding Patterns ◽  
Phosphogluconate Dehydrogenase ◽  
Starch Gel

Forty-five crabapple (Malus spp.) cultivars were evaluated for 16 isozyme systems by starch gel electrophoresis. Of the 16 systems evaluated, 6 were useful in separating among cultivars. Enzyme systems used to distinguish among the cultivars included alcohol dehydrogenase, aspartate aminotransferase, malate dehydrogenase, 6-phosphogluconate dehydrogenase, phosphoglucoisomerase, and shikimate dehydrogenase. Each enzyme system produced one well-resolved polymorphic region except for 6-phosphogluconate dehydrogenase, which produced two. Most crabapple selections could be identified when all six enzymes were evaluated. Alcohol dehydrogenase had the most diagnostic banding patterns useful for cultivar identification.

scholarly journals Inheritance of ADH, 6-PGDH, PGM, and SKDH in Allium fistulosum L.

1994 ◽  
Vol 119 (2) ◽  
pp. 335-338 ◽  
Author(s):  
Paul D. Mangum ◽  
Ellen B. Peffley
Keyword(s):  
Alcohol Dehydrogenase ◽  
Gel Electrophoresis ◽  
Allium Fistulosum ◽  
Starch Gel Electrophoresis ◽  
Shikimate Dehydrogenase ◽  
Chi Square ◽  
Phosphogluconate Dehydrogenase ◽  
Enzyme Systems ◽  
Isozyme Loci ◽  
Starch Gel

Horizontal starch gel electrophoresis was used to study the inheritance of isozyme phenotypes of four enzyme systems [alcohol dehydrogenase (ADH), 6-phosphogluconate dehydrogenase (6-PGDH), phosphoglucomutase (PGM), and shikimate dehydrogenase (SKDH)] in Allium fistulosum L. by monitoring segregations in backcross and F2 progeny. Segregation for most of the polymorphisms fit the expected Mendelian ratios as tested by the chi-square statistic. Three new isozyme loci were defined for onion. Two loci were found for 6-PGDH. Locus one was dimeric with two alleles, and locus two was monomorphic. SKDH was monomeric with two alleles.

scholarly journals A new subunit of horse liver alcohol dehydrogenase and subunit composition of the polymorphic form

1976 ◽  
Vol 153 (2) ◽  
pp. 249-257 ◽  
Author(s):  
R Pietruszko ◽  
C N Ryzewski
Keyword(s):  
Alcohol Dehydrogenase ◽  
Gel Electrophoresis ◽  
Catalytic Properties ◽  
Polymorphic Form ◽  
Subunit Composition ◽  
Starch Gel Electrophoresis ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
Starch Gel

The most cathodal (on starch-gel electrophoresis), steroid-active band of horse liver alcohol dehydrogenase, whose catalytic properties were shown to be dependent on the livers used as a starting material [Pietruszko (1974) Biochem. Biophys. Res. Commun. 60, 687-694], has been prepared from A-type and S-type horse livers by identical methods. Results presented here show that different isoenzymes are present in these preparations.

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.

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