scholarly journals Electrophoretic Patterns of Oxidoreductases and Other Proteins As Criteria in Fungal Taxonomy

1968 ◽  
Vol 21 (2) ◽  
pp. 275 ◽  
Author(s):  
BG Clare ◽  
NT Flentje ◽  
MR Atkinson
Keyword(s):  
Alcohol Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Soluble Proteins ◽  
Fungal Taxonomy ◽  
Electrophoretic Patterns ◽  
Amido Black ◽  
Starch Gel ◽  
Ph Range ◽  
Starch Gels ◽  
Glucose 6 Phosphate Dehydrogenase

Oxidoreductases and other proteins were extracted from fungi and separated by electrophoresis in starch gels. Isolates of FU8arium, Phytophthora, Pythium, Saccharomyces, Schizosaccharomyces, and Thanatephorus (Rhizoctonia) were used. The main soluble proteins were detected by staining with amido black after electrophoresis in starch gel with a discontinuouA citrate-borate system in the pH range 8�2-9�5. Alcohol dehydrogenase (EC 1.1.1.1.), glucose-6-phosphate dehydrogenase (EC 1.1.1.49), malate dehydrogenase (EC 1.1.1.37), diaphorase (i.e. various NADH2-nitro blue tetrazolium oxidoreductases) and

Temperature-dependent enzyme kinetics during avian ontogeny: malate dehydrogenase in the common crow (Corvus brachyrhynchos) and the pintail (Anas acuta)

1973 ◽  
Vol 51 (6) ◽  
pp. 557-565 ◽  
Author(s):  
Michael Aleksiuk
Keyword(s):  
Malate Dehydrogenase ◽  
Kinetic Properties ◽  
Starch Gel Electrophoresis ◽  
Temperature Dependent ◽  
Corvus Brachyrhynchos ◽  
Electrophoretic Patterns ◽  
Specific Effects ◽  
Starch Gel ◽  
The Common ◽  
Species Specific

The electrophoretic patterns and temperature-dependent kinetics of cytoplasmic malate dehydrogenase from liver of juvenile and adult representatives of the common crow (Corvus brachyrhynchos), an altricial species, and the pintail (Anus acuta), a precocial species, were examined. Starch gel electrophoresis revealed two major isoenzymes in each case. The isoenzymes of the juvenile and adult crow exhibit different electrophoretic mobilities, while those of the juvenile and adult pintail exhibit identical mobilities. Assay temperature has no statistically significant age-specific or species-specific effects on several kinetic properties of malate dehydrogenase. In all cases, the Michaelis constant (Km) of oxaloacetate for malate dehydrogenase remains fairly stable below 15 °C, but increases three- to four-fold from 15 ° to 45 °C. Values of activation energy vary between 12.1 and 15.0 kcal/mol. Q10 values for reaction velocities at minimum Km substrate levels are about 1.0 between 30° and 40 °C. The adaptive significance of the observed effects is discussed in relation to poikilothermic stages of the early posthatching ontogeny of birds.

Isoenzymatic pattern of glucose 6-phosphate dehydrogenase from Ascaris suum

1993 ◽  
Vol 67 (3) ◽  
pp. 226-232 ◽  
Author(s):  
C. Cutillas ◽  
B. Rodriguez ◽  
P. German ◽  
D. Guevara
Keyword(s):  
Gel Electrophoresis ◽  
Ascaris Suum ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Starch Gel Electrophoresis ◽  
Specific Staining ◽  
Electrophoretic Patterns ◽  
Starch Gel ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Isoenzymatic Pattern

AbstractThe isoenzymatic pattern of glucose 6-phosphate dehydrogenase (abbreviation G6PD) from Ascaris suum has been studied by vertical polyacrylamide gel (PAGE) and horizontal starch gel electrophoresis. After polyacrylamide gel electrophoresis, two stained zones could be identified. One corresponded to tetrazolium oxidase activity; since this zone was stained even in the absence of glucose 6-phosphate (G6P), non-specific staining could be detected. In the other zone of activity, seven regularly-spaced bands were identified by staining in the presence of G6P and NADP as substrates. By using starch gel electrophoresis, different electrophoretic patterns for G6PD have been observed in the muscular sac, intestine and reproductive system from A. suum. The existence of three different alleles of G6PD in the same individual suggests the existence of at least two genes for this enzyme.

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.

Amine-Citrate Buffers for pH Control in Starch Gel Electrophoresis

1972 ◽  
Vol 29 (8) ◽  
pp. 1169-1172 ◽  
Author(s):  
J. W. Clayton ◽  
D. N. Tretiak
Keyword(s):  
Gel Electrophoresis ◽  
Ph Control ◽  
Starch Gel Electrophoresis ◽  
Good Resolution ◽  
Citrate Buffer ◽  
Starch Gel ◽  
Ph Range ◽  
Amine Buffers

Amine-citrate buffer systems for pH control in starch gel electrophoresis gave good resolution of some dehydrogenase isozymes. The pK's of three new amine buffers, N-(3-aminopropyl)-morpholine, pK2 25 C, 6.12; N-(3-aminopropyl)-diethanolamine, pK2 25 C, 6.90; and 1,3-bis(dimethylamino)-2-propanol, pK2 25 C, 7.55, were determined at 5 C intervals in the range 10–40 C. These compounds, together with N, N-bis(2-hydroxyethyl)iminotris(hydroxymethyl)methane (bis-Tris) and tris-(hydroxymethyl)-methylamine(Tris), provide a series of amine buffers with pK's at 0.5 unit intervals in the pH range 6.1–8.1.

Viscoelastic and textural properties of canary seed starch gels in comparison with wheat starch gel

2019 ◽  
Vol 124 ◽  
pp. 270-281 ◽  
Author(s):  
Mahdi Irani ◽  
Seyed M.A. Razavi ◽  
El-Sayed M. Abdel-Aal ◽  
Pierre Hucl ◽  
Carol Ann Patterson
Keyword(s):  
Textural Properties ◽  
Wheat Starch ◽  
Starch Gel ◽  
Starch Gels

Enzyme variation in the Anopheles gambiae Giles group of species (Diptera: Culicidae)

1978 ◽  
Vol 68 (1) ◽  
pp. 85-97 ◽  
Author(s):  
S. J. Miles
Keyword(s):  
Anopheles Gambiae ◽  
Natural Populations ◽  
Lactic Dehydrogenase ◽  
Starch Gel Electrophoresis ◽  
Malic Dehydrogenase ◽  
Glycerophosphate Dehydrogenase ◽  
Starch Gel ◽  
Anopheles Gambiae Giles ◽  
Species Specific ◽  
Glucose 6 Phosphate Dehydrogenase

AbstractThe genotypes of chromosomally-identified individuals from natural populations of the known species of the group of Anopheles gambiae Giles were scored for the enzyme protein structural loci coding for adenylate kinase (Adk), α-naphthyl acetate esterase (Est-1, Est-2, Est-3), glutamic-oxaloacetic transaminase (Got), α-glycerophosphate dehydrogenase (αGpd), hexokinase (Hk), isocitric dehydrogenase (Idh), lactic dehydrogenase (Ldh), ‘leucine’ aminopeptidase (Lap-2), malic enzyme (Me), octanol dehydrogenase (Odh), phosphoglucomutase (Pgm-1, Pgm-2), 6-phosphogluconic dehydrogenase (6-Pgd), phosphohexose isomerase (Phi) and superoxide dismutase (Sod), following starch gel electrophoresis. In the material examined, Est-1, Est-2, Est-3, Got, ldh, Lap-2, Odh, Pgm-1, Pgm-2 and Sod were segregating for two or more alleles; unique alleles at the Est-1, Got and Sod loci produced species-specific phenotypes in A. melas (Theo.), species C and species D, respectively. The further sampling of A. merus Dön, populations supported the presence of a unique SOD phenotype by which this species can also be identified. Of the other enzyme systems examined, no activity following electrophoresis was detected for aldolase and fructose-1,6-diphosphatase, and the resolution of acid and alkaline phosphatase, glyceraldehyde-3-phosphate dehydrogenase, glucose-6-phosphate dehydrogenase, malic dehydrogenase and xanthine dehydrogenase was too poor under the particular electrophoretic conditions for genetic analyses of the enzyme phenotypes.

scholarly journals MALATE DEHYDROGENASE ISOZYMES OF THE CHICK EMBRYO

1965 ◽  
Vol 13 (6) ◽  
pp. 510-514 ◽  
Author(s):  
JAMES L. CONKLIN ◽  
EDWARD J. NEBEL
Keyword(s):  
Lactate Dehydrogenase ◽  
Chick Embryo ◽  
Malate Dehydrogenase ◽  
Molecular Basis ◽  
Specific Pattern ◽  
Starch Gel Electrophoresis ◽  
Organ Specific ◽  
Malate Dehydrogenase Isozymes ◽  
Starch Gel ◽  
Mitochondrial Malate Dehydrogenase

Malate dehydrogenase fractions of the chick embryo were demonstrated after starch gel electrophoresis of homogenates of liver, brain and spleen. A total of seven malate dehydrogenase fractions were observed to occur in the chick embryo in an organ specific pattern. Treatment of the homogenates with urea, sodium chloride-sodium phosphate, and p-chloromercuribenzoate prior to electrophoresis revealed that only three distinct malate dehydrogenase-active proteins were presence. Two of these proteins exhibited properties similar to those previously reported for the supernatant malate dehydrogenase and mitochondrial malate dehydrogenase of other species. Becuase of the differing properties of chick malate and lactate dehydrogenase it is concluded that the molecular basis for malate dehydrogenase isozymes is different from that reported for lactate dehydrogenase isozymes.

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