Esterase isozyme patterns in Glycine max exposed to gamma radiation

1974 ◽  
Vol 52 (1) ◽  
pp. 273-275 ◽  
Author(s):  
José A. Ferrer-Monge
Keyword(s):  
Glycine Max ◽  
Gamma Radiation ◽  
Gel Electrophoresis ◽  
Soybean Seed ◽  
Starch Gel Electrophoresis ◽  
Esterase Isozyme ◽  
Esterase Isozymes ◽  
Isozyme Patterns ◽  
Starch Gel ◽  
Naphthyl Acetate

The esterase isozyme patterns for irradiated and non-irradiated soybean seed and seedlings were determined by starch gel electrophoresis. Patterns were determined for cotyledons, hypocotyl, epicotyl, first pair of leaves, and roots. Two different esterase systems, E1 and E2, were detected by using appropriate substrates. E1 produces three anodic bands with both α- and β-naphthyl acetate. E2 acts only on α-naphthyl acetate producing three cathodic bands. Radiation did not change the patterns. Results indicate that esterase isozymes are more abundant in the aerial than in the underground portion of developing seedlings.

ESTERASE ISOZYMES IN CANADIAN BARLEY CULTIVARS

1972 ◽  
Vol 52 (4) ◽  
pp. 507-516 ◽  
Author(s):  
GEORGE FEDAK ◽  
TIBOR RAJHATHY
Keyword(s):  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Esterase Isozyme ◽  
Esterase Isozymes ◽  
Isozyme Patterns ◽  
Barley Cultivars ◽  
Starch Gel

Fifty-five currently licensed Canadian cultivars and some parental genotypes were analyzed by starch-gel electrophoresis for esterase isozyme patterns and extent of polymorphism for these isozymes. Each cultivar was assigned to one of nine different patterns observed. Fifty-one percent (28) of the cultivars exhibited polymorphic isozyme patterns. The polymorphism was a varietal characteristic and apparently not associated with the age of the cultivar or area of adaptability.

scholarly journals Genetic variation in the triploids of Japanese Fasciola species, and relationships with other species in the genus

1994 ◽  
Vol 68 (3) ◽  
pp. 181-186 ◽  
Author(s):  
T. Agatsuma ◽  
K. Terasaki ◽  
L. Yang ◽  
D. Blair
Keyword(s):  
United States Of America ◽  
Gel Electrophoresis ◽  
Laboratory Strain ◽  
Morphological Type ◽  
The United States ◽  
Starch Gel Electrophoresis ◽  
Isozyme Patterns ◽  
Electrophoretic Patterns ◽  
Starch Gel ◽  
Liver Flukes

AbstractTwelve enzymes (encoded by 14 loci) in liver flukes of Fasciola species originating from Japan (parthenogenetic triploids), Korea (parthenogenetic diploids), the United States of America (USA) and Australia (all sexual diploids) were analysed using starch gel electrophoresis. Variation in electrophoretic patterns between samples was detected at five enzyme loci (Ak, Got, Gpi, 6-Pgd and Pgm-2). Japanese worms (31, of which six were established as uniparental laboratory strains), which reproduce by parthenogenesis, exhibited three different isozyme patterns. This indicates that triploidy has arisen more than once in Japanese flukes. Japanese Fasciola sp. can be separated into three types on morphological grounds. For the six laboratory strains of Japanese worms, the parental morphological type was known. Each of the three isozyme patterns observed was restricted to one morphological type. Most alleles detected in the Japanese triploids were also found in diploid worms from the other countries: the only alleles not represented elsewhere were four at the Got locus and two at the Pgm locus. Flukes from a laboratory strain derived from a single Korean diploid worm resembled the Japanese worms in genotype more closely than did American (seven uniparental laboratory strains) or Australian (30 worms) specimens. Worms from the last two countries were closely related.

scholarly journals Identifying Pecan Cultivars by Isozymes and Inheritance of Leucine Aminopeptidase

1995 ◽  
Vol 120 (4) ◽  
pp. 661-666 ◽  
Author(s):  
Robert D. Marquard ◽  
Larry J. Grauke ◽  
Tommy E. Thompson ◽  
Ruth S. Janos
Keyword(s):  
Banding Pattern ◽  
Gel Electrophoresis ◽  
Leucine Aminopeptidase ◽  
Phosphoglucose Isomerase ◽  
Starch Gel Electrophoresis ◽  
Carya Illinoensis ◽  
Banding Patterns ◽  
Leaf Material ◽  
Isozyme Patterns ◽  
Starch Gel

More than 170 pecan [Carya illinoensis (Wangenh.) K. Koch] cultivars were evaluated formalate dehydrogenase, phosphoglucose isomerase, phosphoglucomutase, leucine aminopeptidase (LAP), and diaphorase (DIA). Isozymes of LAP were observed in two regions after starch gel electrophoresis. The faster region of activity (Lap-1) was polymorphic and consistently expressed in leaves, wood, and roots. Controlled crosses suggest that Lap-1 is simply inherited and controlled by at least two alleles. DIA was well resolved and storable only from leaf material and produced a complex banding pattern. The ability to differentiate among cultivars by isozymes was good. The 177 cultivars sorted into 72 classes. Forty of the cultivars (23%) possessed a unique series of isozyme patterns. Most cultivars (124 of 177) shared common banding patterns with less than four other cultivars. From the inheritance models of four isozymes, some historical pedigrees can be questioned. Most notably,' Western Schley' could not have been parented by `San Saba' based on the inheritance of Mdh-1 and Lap-1.

Sinapine Esterase. II . Specificity and Change of Sinapine Esterase Activity During Germination of Raphanus sativus

1980 ◽  
Vol 35 (11-12) ◽  
pp. 963-966 ◽  
Author(s):  
Dieter Strack ◽  
Gerhild Nurmann ◽  
Gesine Sachs
Keyword(s):  
Enzyme Activity ◽  
Gel Electrophoresis ◽  
Esterase Activity ◽  
Raphanus Sativus ◽  
Lag Phase ◽  
Starch Gel Electrophoresis ◽  
Rapid Degradation ◽  
Choline Esters ◽  
Starch Gel ◽  
Naphthyl Acetate

Abstract Following a 20 to 24 h lag-phase after sowing, the onset of both rapid degradation of sinapine (sinapolycholine) and rapid increase in sinapine esterase activity in cotyledons of Raphanus sativus was observed. After 2 days of germination maximal enzyme activity was reached and declined in subsequent germination stages as rapidly as it had appeared. Esterases, active against indophenyl acetate, showed highest activity in dry seeds, declining to more than 50% between the 1st and 3rd day of germination. Starch gel electrophoresis showed that all protein extracts contained a multiplicity of esterases, active against α-naphthyl acetate. When gels were incubated with sinapine, one new band appeared, stainable with diazotized ρ-nitroaniline. This band represents sinapine esterase activity. Tests for substrate specificity towards cinnamic acid choline esters showed highest enzyme activity with sinapine. Studies on the occurrence of sinapine esterase in other Brassicaceae revealed that the enzyme activity coincides with the occurrence and degradation of sinapine.

scholarly journals MOUSE ERYTHROCYTE ESTERASES AND AN INTERACTION WITH HEPARIN AS SHOWN BY STARCH GEL ELECTROPHORESIS

1969 ◽  
Vol 17 (2) ◽  
pp. 95-101 ◽  
Author(s):  
McCORMICK TEMPLETON
Keyword(s):  
Young Adult ◽  
Enzymatic Hydrolysis ◽  
Adult Male ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Acetate Esters ◽  
Mouse Erythrocyte ◽  
Starch Gel ◽  
Hydrolysis Of ◽  
Naphthyl Acetate

Esterases from the blood of young adult male C-57 brown mice were separated by starch gel electrophoresis. Enzymatic hydrolysis of the substrates α-naphthyl acetate, naphthyl-AS acetate, α-naphthyl butyrate and acetylthiocholine was studied. Three different esterases were found in erythrocytes. One band hydrolyzed a-naphthyl butyrate but was only slightly active with acetate esters. The fastest migrating bands hydrolyzed acetate faster than butyrate esters, but would hydrolyze both substrates. A third esterase represented in the zymogram by a pair of bands (called "acetate" bands) would hydrolyze only acetate esters. When heparin, or plasma containing heparin, was inserted in a gel so as to overlap an erythrocyte sample, only the acetate bands were altered. When hepanin was inserted cathodal to an erythrocyte sample, the acetate bands are selectively affected by the heparin in such a way as to cause the acetate band to migrate more rapidly toward the anode; other esterase bands were not similarly affected. Acetate bands were not inhibited by physostygmine (1 mM) but their activities diminished with increased concentrations of buffer.

scholarly journals Die Trennung der Hämolymphe-Proteine bei Vorpuppen und Puppen der Galleria mellonella L. mittels Gel-Filtration auf Sephadex G-200, Bestimmung ihrer isoelektrischen Punkte und ihrer Molekulargewichte / Separation of Haemolymph Proteins of Prepuae and Pupae of Galleria mellonella L. by means of Gel Filtration on Sephadex 200, Determination of their Isoelectric Points and their Molecular Weights

1969 ◽  
Vol 24 (6) ◽  
pp. 732-740 ◽  
Author(s):  
Milan Marek
Keyword(s):  
Gel Electrophoresis ◽  
Galleria Mellonella ◽  
Gel Filtration ◽  
Starch Gel Electrophoresis ◽  
Molecular Weights ◽  
Isoelectric Points ◽  
Starch Gel ◽  
The Individual ◽  
Naphthyl Acetate

Gel filtration on Sephadex G-200 was carried out on haemolymph proteins of prepupae. ligatured prepupae, male and female pupae and cooled pupae of Galleria mellonella L.The proteins were separated into two main fractions. The esterase activity of the eluated haemolymph was determined by means of beta-naphthyl acetate after filtration.After elution the samples were condensed and additionally separated on horizontal starch-gel electrophoresis.The “cooling protein” of pupae and the “ligature protein” of ligatured larvae of Galleria mellonella were shown by means of starch-gel electrophoresis to be new proteins, so far not described.The isoelectric point and molecular weight were determined for the individual protein fractions.They were then stained with amido black 10 B for the proof of proteins, and with alpha-naphthyl butyrate with Fast-Blue BB salt for the identification of esterases.

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.

Sign in / Sign up

Export Citation Format

Share Document