Characterization of isoperoxidase activity in Arachis hypogaea cultivars

Cherry, John P.; Ory, Robert L.

doi:10.1016/0031-9422(73)80371-1

Cited by 13 publications

(6 citation statements)

References 10 publications

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“…Figs. 1,6,8). Much intra-and/or interspecific polymorphism was noted for the proteins and enzymes of these seeds making it difficult to determine the chemotaxonomy of this section (Figs.…”

Section: Section Rhizomatosaementioning

confidence: 99%

Comparative Studies of Seed Proteins and Enzymes of Species and Collections of Arachis by Gel Electrophoresis

Cherry

1975

Peanut Science

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Proteins and six enzymes (esterase, peroxidase, catalase, leucine aminopeptidase, alcohol dehydrogenase, achromatic oxidase) in individual seeds from 36 species and collections of Arachis were characterized by using polyacrylamide and starch gel electrophoretic techniques. These data were used to evaluate the biosystematics of Arachis. Support was found for the thesis that each wild relative of the cultivated peanut, Arachis hypogaea L., has been properly classified into coherent groups of species under the following taxonomic sections: Axonomorphae, Erectoides, Caulorhizae, Rhizomatosae, Extranervosae, Pseudoaxonomorphae and Triseminalae. For example, the mobility of most bands in the gel patterns of proteins and enzymes of A. hypogaea coincided very closely with those of the wild species, A. monticola PI 219824, supporting studies which have shown that these two species are closely related and should be classified together. The Similarity Index method, based upon the percent of protein and enzyme bands with similar and dissimilar mobilities compared among gels of seeds of species and collections, produced s-values that further supported the taxonomy of this genus as it is known today.

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“…Figs. 1,6,8). Much intra-and/or interspecific polymorphism was noted for the proteins and enzymes of these seeds making it difficult to determine the chemotaxonomy of this section (Figs.…”

Section: Section Rhizomatosaementioning

confidence: 99%

Comparative Studies of Seed Proteins and Enzymes of Species and Collections of Arachis by Gel Electrophoresis

Cherry

1975

Peanut Science

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“…This date shows a large genetic uniformity for LAP in peanuts. Monomorphic LAP patterns were also observed in peanuts by Cherry & Ory (1973a) and Grieshammer & Wynne (1990).…”

Section: Resultsmentioning

confidence: 76%

“…Qualitative and quantitative isoenzymatic analysis have been utilized in biochemical, physiological, chemotaxonomy and genetic variability investigation in a large number of plant populations, cultivars and species (Cherry & Ory, 1973a;Fedak, 1974;Huhns & Fretz, 1978;Nielsen & Johansen, 1986;Ramirez et al, 1986).…”

Section: Introductionmentioning

confidence: 99%

Avaliação da variabilidade isoenzimática de cinco cultivares de amendoim

Galgaro

Lopes

1994

Bragantia

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Genetic variability within and among different samples of peanut (Arachis hypogaea L.) from the cultivars Roxo, Tatu Branco, Tatu Vermelho, Tatuí Vermelho and Tatuí (white skin seeds) was evaluated using polyacrilamide gel electrophoresis by studying leucine aminopeptidase (LAP), aspartate aminotransferase (ATT) and peroxidase (PER) enzymatic systems. Seeds were obtained from local farms located in Marília, Presidente Prudente and São Manuel cities, State of São Paulo, Brazil. Three enzymatic bands called LAP-A, LAP-B and LAP-C were observed in the patterns of the leucine aminopeptidase. Aspartate aminotransferase patterns showed three anodic bands, AAT-A, AAT-B and AAT-C. The peroxidase system showed fifteen bands, including eight anodics (PER-A to PER-H) and seven cathodics (PER-I to PER-P). The peroxidase and leucine aminopeptidase enzymatic systems were not discriminative among the different samples from the five cultivars analysed. Only the aspartate aminotransferase enzymatic system showed one characteristic pattern compound by AAT-B and AAT-C bands. This pattern was observed in Tatu Branco from Presidente Prudente and Tatuí Vermelho from Presidente Prudente and São Manuel.

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“…Peroxidase activity has been studied extensively by disc gel electrophoresis in several varieties of peanuts grown in different geographic areas (4,5). Five major isozyme patterns from mature peanuts comprised 78% of the 15 different patterns observed for 15 different varieties of Virginia, Spanish, and Runner peanuts examined (4).…”

Section: Effects Of Additives In Watermentioning

confidence: 99%

Effect of minor constituents and additives upon peroxidation of oil in peanut butter

Angelo

Ory

1975

J Americ Oil Chem Soc

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Metalloproteins and ionic iron and copper salts are major catalysts of fatty acid peroxidation, but chelating agents, such as ethylenediaminetetraacetic acid and citric acid in water, can retard or reduce this catalytic effect. To extend shelf-life and retain the high quality of peanut butter, methods to prevent or decrease the catalytic effect of these metalloproteins and salts were conducted. Chelating agents suspended in inert solvents (mineral oil) were not as effective as when they were added in water. Depending upon the concentration, water can act as a prooxidant or an antioxidant in peanut butter.

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Characterization of isoperoxidase activity in Arachis hypogaea cultivars

Cited by 13 publications

References 10 publications

Comparative Studies of Seed Proteins and Enzymes of Species and Collections of Arachis by Gel Electrophoresis

Comparative Studies of Seed Proteins and Enzymes of Species and Collections of Arachis by Gel Electrophoresis

Avaliação da variabilidade isoenzimática de cinco cultivares de amendoim

Effect of minor constituents and additives upon peroxidation of oil in peanut butter

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