r amygdalin/prunus serotina

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8 torthaí

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

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Logáil Isteach / Cláraigh

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

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

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Logáil Isteach / Cláraigh

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

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

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Logáil Isteach / Cláraigh

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

Utilization of Amygdalin during Seedling Development of Prunus serotina.

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Logáil Isteach / Cláraigh

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 Level Compartmentation of (R)-Amygdalin and Amygdalin Hydrolase Prevents Large-Scale Cyanogenesis in Undamaged Prunus Seeds.

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Logáil Isteach / Cláraigh

Plum (Prunus domestica) seeds, which contain the cyanogenic diglucoside (R)-amygdalin and lesser amounts of the corresponding monoglucoside (R)-prunasin, release the respiratory toxin HCN upon tissue disruption. Amygdalin hydrolase (AH) and prunasin hydrolase (PH), two specific [beta]-glucosidases

Temporal and spatial expression of amygdalin hydrolase and (R)-(+)-mandelonitrile lyase in black cherry seeds.

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Logáil Isteach / Cláraigh

In black cherry (Prunus serotina Ehrh.) macerates, the cyanogenic diglucoside (R)-amygdalin undergoes stepwise degradation to HCN catalyzed by amygdalin hydrolase (AH), prunasin hydrolase, and (R)-(+)-mandelonitrile lyase (MDL). A near full-length AH cDNA clone (pAH1), whose insert encodes the

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

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Logáil Isteach / Cláraigh

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

Localization and catabolism of cyanogenic glycosides.

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Logáil Isteach / Cláraigh

The catabolism of cyanogenic glycosides is initiated by cleavage of the carbohydrate moiety by one or more beta-glycosidases, which yields the corresponding alpha-hydroxynitrile. Until recently, the mode by which cyanogenic disaccharides are hydrolysed was largely unclear. Investigation of highly

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