Isozymes of amylase, alcohol dehydrogenase, malic enzyme, malate dehydrogenase, and superoxide dismutase in Chloealtis conspersa (Orthoptera)

Genome ◽  
1989 ◽  
Vol 32 (4) ◽  
pp. 596-600 ◽  
Author(s):  
Peter B. Moens ◽  
Steven Kolodziejczyk
Keyword(s):  
Superoxide Dismutase ◽  
Alcohol Dehydrogenase ◽  
Malate Dehydrogenase ◽  
X Chromosome ◽  
Gel Electrophoresis ◽  
Malic Enzyme ◽  
Duplicate Genes ◽  
Gene Linkage ◽  
Slow Band

Five enzymes of the grasshopper Chloealtis conspersa were studied for possible gene linkage. Because of the extreme localization of chiasmata throughout most of the genome of C. conspersa, it was expected that genes would appear either to be completely linked or to assort independently. Our results indicate that malic enzyme and alcohol dehydrogenase are probably on the X chromosome. Superoxide dismutase is produced from the product of duplicate genes where Sod 1-1 is monomorphic and Sod 1-2 has two alleles, one producing a fast-migrating band on gel electrophoresis and one a slow band. While amylase, malate dehydrogenase, and superoxide dismutase appeared to be autosomal, there was no evidence of linkage between them.Key words: Chloealtis conspersa, amylase, alcohol dehydrogenase, malic enzyme, malate dehydrogenase, superoxide dismutase.

scholarly journals Expression of Enzymes During the Germination of Seeds in Endangered Cerrado Species

2019 ◽  
Vol 11 (6) ◽  
pp. 469
Author(s):  
J. G. R. Assis ◽  
E. R. Marques ◽  
M. L. M. Carvalho ◽  
R. M. O. Pires ◽  
C. A. Lopes ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Alcohol Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Germination Test ◽  
C Elegans ◽  
Germination Process ◽  
Germination Speed ◽  
Normal Seedling ◽  
Radicle Protrusion ◽  
Seeds Germination

The objective of this study was to evaluate the enzymes expression during the seeds germination process of ever-lasting species Comanthera elegans and Comanthera bisulcata. For the evaluation of the seeds physiological potential, the germination test and index of germination speed were performed. The expression of enzymes esterase (EST), malate dehydrogenase (MDH), alcohol dehydrogenase (ADH), superoxide dismutase (SOD), catalase (CAT) and endo-β-mannanase during the germination process were evaluated. The expression of these enzymes was evaluated in dried seeds, in the protrusion, in the emergence of the primal leaf, at the beginning of the formation of normal seedling and dormant seeds at the end of the germination process. To the extent that the germination process occurs in the species C. bisulcata and C. elegans there is greater expression of the enzyme CAT and lower of the enzyme EST. There is variation in the expression of the enzymes SOD, ADH and MDH in seeds of both species during the germination process. The enzyme endo-β-mannanase presents greater activity in seeds with radicle protrusion in the two studied species.

scholarly journals HARVEST TIMES WITH CHEMICAL DESICCATION AND THE EFFECTS ON THE ENZYMATIC EXPRESSION AND PHYSIOLOGICAL QUALITY OF SOYBEAN SEEDS

2020 ◽  
Vol 33 (2) ◽  
pp. 361-370
Author(s):  
ALAN MARIO ZUFFO ◽  
JORGE GONZÁLEZ AGUILERA ◽  
EVERSON REIS CARVALHO ◽  
PAULO EDUARDO TEODORO
Keyword(s):  
Superoxide Dismutase ◽  
Alcohol Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Isocitrate Lyase ◽  
Soybean Seeds ◽  
Phenological Stage ◽  
Physiological Quality ◽  
Physiological Tests ◽  
Enzymatic Expression

ABSTRACT This study aimed to evaluate the effect of chemical desiccants and harvest times on the enzymatic expression and physiological quality of soybean seeds. The experiment was carried out in a randomized block design with four replications, in a factorial scheme (4 × 3 + 1) with four desiccants (paraquat - 2 L ha-1, ammonium glufosinate - 2 L ha-1, diquat - 1.5 L ha-1, and saflufenacil - 40 g ha-1). These were applied at the phenological stage R7.1 (beginning of leaf yellowing) and at three harvest times (0, 14, and 28 days after the phenological stage R8). There was also a control treatment (no desiccant, harvested at R8). The physiological quality of soybean seeds and the enzymatic expressions of malate dehydrogenase, alcohol dehydrogenase, esterase, isocitrate lyase, and superoxide dismutase were evaluated in laboratory tests. Seeds harvested at the R8 + 14 stage led to the highest losses in seed quality. However, the 50 mm rainfall also affected seed deterioration. The desiccants diquat and paraquat provided the lowest and the highest damage to the seed physiological quality, respectively. The expression of the enzymes alcohol dehydrogenase, esterase, and isocitrate lyase were efficient and had an adequate correlation with the physiological quality. Malate dehydrogenase and superoxide dismutase had no satisfactory relation with the physiological tests performed with soybean seeds.

scholarly journals Vigor tests for evaluation of crambe (Crambe abyssinica Hochst) seed quality

2013 ◽  
Vol 35 (4) ◽  
pp. 485-494 ◽  
Author(s):  
Sara Michelly Cruz ◽  
Marcela Carlota Nery ◽  
Adriana de Souza Rocha ◽  
Édila Vilela de Resende Von Pinho ◽  
Paulo César de Resende Andrade ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Alcohol Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Seed Quality ◽  
Isocitrate Lyase ◽  
Accelerated Aging ◽  
Crambe Abyssinica ◽  
Accelerated Aging Test ◽  
Aging Test ◽  
Dehydrogenase Enzyme

The aim of this study was adapting the methodology of the accelerated aging test (AA) and electrical conductivity test (EC) to evaluate seed quality of crambe, as well as verifying enzymatic activity in relation to vigor differences. Crambe seed lots, cv. FMS Brilhante, were evaluated by the AA test, for periods of 0, 24, 48, 72 and 96 h, at 42 °C, with and without NaCl saturated solution; and the EC test, by soaking seeds into deionized water (mL) in the ratios of 25/25, 25/50, 50/50 and 50/75 (seed/water) for 2, 4, 6, 8, 10, 12, 14, 16 and 18 h. The electrophoretic profile for isozymes esterase, superoxide dismutase, catalase, isocitrate lyase, alcohol dehydrogenase and malate dehydrogenase was evaluated on polyacrylamide gel (7.5%). The AA test conducted at 42 °C, for 96 h, was efficient to detect differences on seed quality levels; however, the EC test was not suitable to evaluate vigor of those seeds. The bands stained for isozymes esterase, superoxide dismutase and catalase were evident for the more vigorous seeds; and the bands for isozymes isocitrate lyase and alcohol dehydrogenase were less evident for the less vigorous seeds. For enzyme malate dehydrogenase enzyme intensity of bands was similar.

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.

scholarly journals Biochemical changes and physiological quality of corn seeds subjected to different chemical treatments and storage times

2020 ◽  
Vol 42 ◽  
Author(s):  
Thiago Lucas de Oliveira ◽  
Renzo Garcia Von Pinho ◽  
Heloisa Oliveira dos Santos ◽  
Karen Marcelle de Jesus Silva ◽  
Elise de Matos Pereira ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Alcohol Dehydrogenase ◽  
Cold Test ◽  
Chemical Treatments ◽  
Treatment Standard ◽  
Quality Markers ◽  
Physiological Quality ◽  
Storage Times ◽  
And Storage

Abstract: The chemical treatment of corn seeds is widely adopted for protecting crops at the early stages. However, some molecules interfere in the quality of seeds, especially when stored, by accelerating their deterioration. The objective of this work was to investigate the influence of insecticides on the enzymatic expression and quality of corn seeds subjected to storage. Seeds of the hybrids 2B647PW and SHS4070 were subjected to four different chemical treatments (standard treatment, standard + clothianidin, standard + thiamethoxam, and standard + fipronil) and stored for different periods (0, 3, 6, and 9 months). The quality evaluation included the germination test, first germination count, cold test, and health test. The expression of the enzymes α-amylase, esterase, superoxide dismutase, catalase, and alcohol dehydrogenase were determined by the gel electrophoresis technique. The insecticides clothianidin, thiamethoxam, and fipronil reduce the physiological quality of the seeds of hybrid 2B647PW after nine months of storage. The treatment of seeds with the insecticides clothianidin, thiamethoxam, and fipronil reduces the expression of α-amylase, superoxide dismutase, and catalase enzymes after nine months of storage. The enzymes α-amylase, superoxide dismutase, catalase, and alcohol dehydrogenase are good quality markers for hybrid corn seeds.

Regulation of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (AldDH) in Aspergillus nidulans

1983 ◽  
Vol 217 (1208) ◽  
pp. 243-264 ◽  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Aspergillus Nidulans ◽  
Structural Gene ◽  
Aldehyde Dehydrogenase ◽  
Gel Electrophoresis ◽  
Regulatory Gene ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Wild Type ◽  
Cell Extracts

There is a single major alcohol dehydrogenase (ADH) and a single major aldehyde dehydrogenase (AldDH) in Aspergillus nidulans . Both ADH and AldDH are induced by ethanol and by acetaldehyde and both are subject to carbon catabolite repression. ADH and AldDH are necessary for the utilization of ethanol and of threonine, indicating that both compounds are utilized via acetaldehyde. ADH and AldDH each give a single major activity band on gel electrophoresis. Sodium dodecyl sulphate polyacrylamide gel electrophoresis of cell extracts shows at least two similar ADH polypeptides of approximate relative molecular mass (r. m. m.) 41000 and two similar AldDH polypeptides of approximate r. m. m. 57000. The in vitro translation of mRNA from induced, carbon derepressed wild-type cells gives up to three ADH polypeptides in the r. m. m. range 39000-43000 and an AldDH polypeptide of approximate r. m. m. 57000. The mRNA from uninduced, carbon repressed wild-type cells does not direct the synthesis of the ADH and AldDH polypeptides. This indicates that the regulation of ADH and AldDH is at the level of transcription and/or post-transcriptional modification. The probable explanation of the multiple ADH polypeptides is post-transcriptional modification of the mRNA. Allyl alcohol mutants were made by using diepoxyoctane and γ-rays as mutagens. There are two classes, alcA and alcR . Neither class can utilize ethanol or threonine as a carbon source. The alcA mutants lack normal ADH and are recessive. Of the 47 alcA mutants examined 39 do not make the ADH polypeptides while eight do so. Therefore alcA is the structural gene for ADH. The two alcA mutants tested do not make functional mRNA for ADH. The alcR mutants lack both ADH and AldDH and are recessive. No alcR mutants make the ADH or the AldDH polypeptides. The three alcR mutants tested do not make functional ADH or AldDH mRNA. The mutant alcR 125 is a nonsense mutant, which establishes that alcR codes for a protein. The alcA and alcR genes are adjacent on chromosome VII and a preliminary fine-structure map of the alcA gene has been made. Three mutants that cannot utilize ethanol or threonine and have ADH, but lack AldDH, define a gene AldA on chromosome VIII. The aldA 23 mutant makes the AldDH polypeptides, the other two aldA mutants do not. Therefore aldA is probably the structural gene for AldDH. Our current hypothesis is that alcA and aldA are the structural genes for ADH and AldDH respectively and alcR is a transacting regulatory gene coding for a protein whose function is necessary for the expression of the alcA and aldA genes.

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