glucosidase/kukurūza

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Kinetics of α-amylase and α-glucosidase inhibitory potential of Zea mays Linnaeus (Poaceae), Stigma maydis aqueous extract: An in vitro assessment.

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Ielogoties Reģistrēties

BACKGROUND Corn silk (Zea mays L., Stigma maydis) is an important herb used traditionally in many parts of the world to treat array of diseases including diabetes mellitus. Inhibitors of α-amylase and α-glucosidase offer an effective strategy to modulate levels of post prandial hyperglycaemia via

Characterization of two membrane-associated beta-glucosidases from maize (Zea mays L.) coleoptiles.

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Ielogoties Reģistrēties

We isolated membrane vesicles from maize (Zea mays L.) coleoptiles and identified in these vesicles a 58 kDa (pm58) and a 60 kDa (pm60) protein by photoaffinity labelling with 5-azido-[7-3H]indole-3-acetic acid ([3H]N3IAA). Photoaffinity labelling was effectively competed for by auxins as well as by

Purification and Partial Characterization of Maize (Zea mays L.) beta-Glucosidase.

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Ielogoties Reģistrēties

Maize (Zea mays L.) beta-glucosidase (beta-d-glucoside glucohydrolase, EC 3.2.1.21) was extracted from the coleoptiles of 5- to 6-day-old maize seedlings with 50 millimolar sodium acetate, pH 5.0. The pH of the extract was adjusted to 4.6, and most of the contaminating proteins were cryoprecipitated

Genome-wide analysis of the beta-glucosidase gene family in maize (Zea mays L. var B73).

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Ielogoties Reģistrēties

The hydrolysis of beta-D: -glucosidic bonds which is required for the liberation of many physiologically important compounds is catalyzed by the enzyme beta-glucosidase (BGLU, EC 3.2.1.21). BGLUs are implicated in several processes in plants, such as the timely response to biotic and abiotic

Genetic control and racial variation of beta-glucosidase isozymes in maize (Zea mays L.)

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Ielogoties Reģistrēties

beta-Glucosidase (beta-D-glucoside glucohydrolase, E.C. 3.2.1.21, beta-Glu) isozyme variants were studied in a large number of inbred lines, crosses, and races of maize (Zea mays L.). The pattern of Mendelian inheritance demonstrated for beta-GLU variants indicated that they are under nuclear gene

A novel beta-glucosidase from the cell wall of maize (Zea mays L.): rapid purification and partial characterization.

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Ielogoties Reģistrēties

Plants have a variety of glycosidic conjugates of hormones, defense compounds, and other molecules that are hydrolyzed by beta-glucosidases (beta-D-glucoside glucohydrolases, E.C. 3.2.1.21). Workers have reported several beta-glucosidases from maize (Zea mays L.; Poaceae), but have localized them

Antioxidant, α-glucosidase and xanthine oxidase inhibitory activity of bioactive compounds from maize (Zea mays L.).

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Chemical investigations into maize (Zea mays L.) kernels yielded phenolic compounds, which were structurally established using chromatographic and spectroscopic methods. The isolated phenolic compounds from maize kernel were examined in vitro for their antioxidant abilities by DPPH

Herbivore-induced volatiles: the emission of acyclic homoterpenes from leaves of Phaseolus lunatus and Zea mays can be triggered by a beta-glucosidase and jasmonic acid.

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Ielogoties Reģistrēties

The treatment of healthy, undamaged plants of the Lima bean Phaseolus lunatus with solutions of a beta-glucosidase from bitter almonds (at 5 U.ml-1) through the petiole results in an enhanced emission of volatiles to the environment. The compounds are identical with those emitted in response to

Corn silk (Zea mays L.), a source of natural antioxidants with α-amylase, α-glucosidase, advanced glycation and diabetic nephropathy inhibitory activities.

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Ielogoties Reģistrēties

The oxidative stress plays a critical role in the progression of diabetes mellitus (DM) and its complications. Corn silk is a traditional medicine used to treat DM. The aim of this study is to investigate the antioxidant capacity of corn silk, as well as its inhibitory potential on DM and diabetic

Histochemical localization of beta-glycosidases in roots of Zea mays. I. A simultaneous coupling azo-dye technique for the localization of beta-glucosidase and beta-galactosidase.

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A specific beta-glucosidase-aggregating factor is responsible for the beta-glucosidase null phenotype in maize.

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Ielogoties Reģistrēties

Maize (Zea mays L.) beta-glucosidase was extracted from shoots of a wild-type (K55) and a "null" (H95) maize genotype. Enzyme activity assays and electrophoretic data showed that extracts from the null genotype had about 10% of the activity present in the normal genotype. Zymograms of the null

Induction of beta-glucosidase activity in maize coleoptiles by blue light illumination.

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Ielogoties Reģistrēties

The role of beta-glucosidase during the phototropic response in maize (Zea mays) coleoptiles was investigated. Unilateral blue light illumination abruptly up-regulated the activity of beta-glucosidase in the illuminated halves, 10 min after the onset of illumination, peaking after 30 min and

Functional analysis of the aglycone-binding site of the maize beta-glucosidase Zm-p60.1.

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Ielogoties Reģistrēties

Beta-glucosidases such as Zm-p60.1 (Zea mays) and Bgl4:1 (Brassica napus) have implicated roles in regulating plant development by releasing biologically active cytokinins from O-glucosides. A key determinant of substrate specificity in Zm-p60.1 is the F193-F200-W373-F461 cluster. However, despite

Insights into the functional architecture of the catalytic center of a maize beta-glucosidase Zm-p60.1.

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Ielogoties Reģistrēties

The maize (Zea mays) beta-glucosidase Zm-p60.1 has been implicated in regulation of plant development by the targeted release of free cytokinins from cytokinin-O-glucosides, their inactive storage forms. The crystal structure of the wild-type enzyme was solved at 2.05-A resolution, allowing

Substrate (aglycone) specificity of human cytosolic beta-glucosidase.

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Ielogoties Reģistrēties

Human cytosolic beta-glucosidase (hCBG) is a xenobiotic-metabolizing enzyme that hydrolyses certain flavonoid glucosides, with specificity depending on the aglycone moiety, the type of sugar and the linkage between them. Based upon the X-ray structure of Zea mays beta-glucosidase, we generated a

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