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Quantitative analysis of amygdalin and prunasin in Prunus serotina Ehrh. using (1) H-NMR spectroscopy.

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BACKGROUND Prunus serotina is native to North America but has been invasively introduced in Europe since the seventeenth century. This plant contains cyanogenic glycosides that are believed to be related to its success as an invasive plant. For these compounds, chromatographic- or

Immunocytochemical Localization of Prunasin Hydrolase and Mandelonitrile Lyase in Stems and Leaves of Prunus serotina.

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In macerates of black cherry (Prunus serotina Ehrh.) leaves and stems, (R)-prunasin is catabolized to HCN, benzaldehyde, and D-glucose by the sequential action of prunasin hydrolase (EC 3.2.1.21) and (R)-(+)-mandelonitrile lyase (EC 4.1.2.10). Immuno-cytochemical techniques have shown that within

Prunus serotina Amygdalin Hydrolase and Prunasin Hydrolase : Purification, N-Terminal Sequencing, and Antibody Production.

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In black cherry (Prunus serotina Ehrh.) seed homogenates, amygdalin hydrolase (AH) participates with prunasin hydrolase (PH) and mandelonitrile lyase in the sequential degradation of (R)-amygdalin to HCN, benzaldehyde, and glucose. Four isozymes of AH (designated AH I, I', II, II') were purified

Isolation and characterization of multiple forms of prunasin hydrolase from black cherry (Prunus serotina Ehrh.) seeds.

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Three forms of prunasin hydrolase (PH I, PH IIa, and PH IIb), which catalyze the hydrolysis of (R)-prunasin to mandelonitrile and D-glucose, have been purified from homogenates of mature black cherry (Prunus serotina Ehrh.) seeds. Hydroxyapatite chromatography completely resolved PH I from PH IIa

Occurrence of Benzoic Acid Esters as Putative Catabolites of Prunasin in Senescent Leaves of Prunus laurocerasus.

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Prunus laurocerasus is an evergreen shrub containing large quantities of the cyanogenic glycoside prunasin (1) in its leaves, which decomposes to prunasin amide (2) or glucose-1-benzoate (4) when the leaves become chlorotic as a result of senescence or pseudosenescence. This study was aimed at the

Investigation of the microheterogeneity and aglycone specificity-conferring residues of black cherry prunasin hydrolases.

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In black cherry (Prunus serotina Ehrh.) seed homogenates, (R)-amygdalin is degraded to HCN, benzaldehyde, and glucose by the sequential action of amygdalin hydrolase (AH), prunasin hydrolase (PH), and mandelonitrile lyase. Leaves are also highly cyanogenic because they possess (R)-prunasin, PH, and

Seasonal Changes Affect Root Prunasin Concentration in Prunus serotina and Override Species Interactions between P. serotina and Quercus petraea.

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The allocation of resources to chemical defense can decrease plant growth and photosynthesis. Prunasin is a cyanogenic glycoside known for its role in defense against herbivores and other plants. In the present study, fluctuations of prunasin concentrations in roots of Prunus serotina seedlings were

Prunasin production using engineered Escherichia coli expressing UGT85A47 from Japanese apricot and UDP-glucose biosynthetic enzyme genes.

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Japanese apricot, Prunus mume Sieb. et Zucc., biosynthesizes the l-phenylalanine-derived cyanogenic glucosides prunasin and amygdalin. Prunasin has biological properties such as anti-inflammation, but plant extraction and chemical synthesis are impractical. In this study, we identified and

Prunasin hydrolases during fruit development in sweet and bitter almonds.

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Amygdalin is a cyanogenic diglucoside and constitutes the bitter component in bitter almond (Prunus dulcis). Amygdalin concentration increases in the course of fruit formation. The monoglucoside prunasin is the precursor of amygdalin. Prunasin may be degraded to hydrogen cyanide, glucose, and

Comparison of kinetic and molecular properties of two forms of amygdalin hydrolase from black cherry (Prunus serotina Ehrh.) seeds.

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Two forms of the beta-glucosidase amygdalin hydrolase (AH I and II), which catalyze the hydrolysis of (R)-amygdalin to (R)-prunasin and D-glucose, have been purified over 200-fold from mature black cherry (Prunus serotina Ehrh.) seeds. These proteins showed very similar molecular and kinetic

A seed coat cyanohydrin glucosyltransferase is associated with bitterness in almond (Prunus dulcis) kernels

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The secondary metabolite amygdalin is a cyanogenic diglucoside that at high concentrations is associated with intense bitterness in seeds of the Rosaceae, including kernels of almond (Prunus dulcis (Mill.), syn. Prunus amygdalus D. A. Webb Batsch). Amygdalin is a glucoside of prunasin, itself a

Erratum to: A seed coat cyanohydrin glucosyltransferase is associated with bitterness in almond (Prunus dulcis) kernels

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Utilization of Amygdalin during Seedling Development of Prunus serotina.

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Cotyledons of mature black cherry (Prunus serotina Ehrh.) seeds contain the cyanogenic diglucoside (R)-amygdalin. The levels of amygdalin, its corresponding monoglucoside (R)-prunasin, and the enzymes that metabolize these cyanoglycosides were measured during the course of seedling development.

Tissue and Subcellular Localization of Enzymes Catabolizing (R)-Amygdalin in Mature Prunus serotina Seeds.

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In black cherry (Prunus serotina Ehrh.) homogenates, (R)-amygdalin is catabolized to HCN, benzaldehyde, and d-glucose by the sequential action of amygdalin hydrolase, prunasin hydrolase, and mandelonitrile lyase. The tissue and subcellular localizations of these enzymes were determined within intact

Development of the Potential for Cyanogenesis in Maturing Black Cherry (Prunus serotina Ehrh.) Fruits.

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Biochemical changes related to cyanogenesis (hydrogen cyanide production) were monitored during maturation of black cherry (Prunus serotina Ehrh.) fruits. At weekly intervals from flowering until maturity, fruits (or selected parts thereof) were analyzed for (a) fresh and dry weights, (b) prunasin

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