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Sida 1 från 93 resultat
Alliin lyase (Alliinase) from garlic (Allium sativum). Biochemical characterization and cDNA cloning.
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The garlic plant (Allium sativum) alliinase (EC 4.4.1.4), which catalyzes the synthesis of allicin, was purified to homogeneity from bulbs using various steps, including hydrophobic chromatography. Molecular and biochemical studies showed that the enzyme is a dimer of two subunits of MW 51.5 kDa
Isolation and characterization of alliinase cDNA clones from garlic (Allium sativum L.) and related species.
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cDNA libraries constructed from poly(A)-rich RNA isolated from Allium sativum (garlic), Allium cepa (onion) and Allium ascalonicum (shallot) were screened for cDNA clones encoding the alliinase using colony hybridization. Sequence analysis of the alliinase cDNA clones from different Alliaceae
Purification, characterization, and crystallization of alliinase from garlic.
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Glycosylated dimeric alliinase (EC 4.4.1.4) was purified to homogeneity from its natural source, garlic. With 660 units/mg, the specific enzymatic activity of the pure enzyme is the highest reported to date. Based on both CD spectroscopy data and sequence-derived secondary structure prediction, the
Thiol-disulfide organization in alliin lyase (alliinase) from garlic (Allium sativum).
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Alliinase, an enzyme found in garlic, catalyzes the synthesis of the well-known chemically and therapeutically active compound allicin (diallyl thiosulfinate). The enzyme is a homodimeric glycoprotein that belongs to the fold-type I family of pyridoxal-5'-phosphate-dependent enzymes. There are 10
Isolation and characterization of lectins and lectin-alliinase complexes from bulbs of garlic (Allium sativum) and ramsons (Allium ursinum).
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A procedure developed to separate the homodimeric and heterodimeric mannose-binding lectins from bulbs of garlic (Allium sativum L.) and ramsons (Allium ursinum L.) also enabled the isolation of stable lectin-alliinase complexes. Characterization of the individual lectins indicated that, in spite of
Alliin lyase (alliinase) from garlic (Allium sativum): crystallization and preliminary X-ray characterization.
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The enzyme alliinase has been isolated from garlic bulbs and crystallized. The crystals belong to space group P2(1), with unit-cell parameters a = 70.191, b = 127.006, c = 108.085 A, beta = 93.384 degrees. They diffract to 2.2 A at liquid-nitrogen temperature. Analysis of the Patterson self-rotation
Low-frequency and low-intensity ultrasound accelerates alliinase-catalysed synthesis of allicin in freshly crushed garlic.
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BACKGROUND
The well-known chemically and therapeutically active compound allicin is formed in crushed garlic by the interaction of alliin with alliinase. In this study, low-frequency and low-intensity ultrasound was employed to accelerate the alliinase-catalysed synthesis of allicin in freshly
Alliinase (alliin lyase) from garlic (Alliium sativum) is glycosylated at ASN146 and forms a complex with a garlic mannose-specific lectin.
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Alliinase (EC 4.4.1.4) catalyses the production of allicin (thio-2-propene-1-sulfinic acid S-allyl ester), a biologically active compound which is also responsible for the characteristic smell of garlic. It was demonstrated that alliinase which contains 5.5-6% of neutral sugars, gives clear
'Laba' garlic processed by dense phase carbon dioxide: the relation between green colour generation and cellular structure, alliin consumption and alliinase activity.
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BACKGROUND
'Laba' garlic is usually processed by soaking garlic in vinegar for more than 1 week during winter. It is popular for its unique green colour and tasty flavour. Greening is desirable and required for this product as its characteristic. Dense phase carbon dioxide (DPCD) had a significant
Developmental Regulation of Lectin and Alliinase Synthesis in Garlic Bulbs and Leaves.
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Using a combination of northern blot analysis and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, a detailed study was made of the temporal and spatial regulation of garlic (Allium sativum L.) lectins and alliinase throughout the life cycle of the plant. The two bulb-specific lectins
Quality of herbal remedies from Allium sativum: differences between alliinase from garlic powder and fresh garlic.
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Alliinase (EC 4.4.1.4) has been isolated from commercially available garlic (Allium sativum L., Alliaceae) powder and was investigated with respect to its use as ingredient of herbal remedies. The enzyme was purified to apparent homogeneity and results were compared with those obtained from a sample
Distinct intraspecific variations of garlic (Allium sativum L.) revealed by the exon-intron sequences of the alliinase gene.
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Garlic (Allium sativum L.) has been used worldwide as a food and for medicinal purposes since early times. Garlic cultivars exhibit considerable morphological diversity despite the fact that they are mostly sterile and are grown only by vegetative propagation of cloves. Considerable recombination
Garlic (A. sativum L.) alliinase gene family polymorphism reflects bolting types and cysteine sulphoxides content.
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BACKGROUND
Alliinase is an important enzyme occurring in Allium species that converts precursors of sulfuric compounds, cysteine sulfoxides into a biologically active substance termed allicin. Allicin facilitates garlic defense against pests and produces health-promoting compounds. Alliinase is
Low allicin release from garlic supplements: a major problem due to the sensitivities of alliinase activity.
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Most garlic supplements are standardized on allicin potential and are enteric-coated to prevent gastric acid inactivation of the allicin-producing enzyme, alliinase. To determine whether these products release the claimed amount of allicin under simulated gastrointestinal conditions, USP dissolution
Alliinase and cysteine synthase transcription in developing garlic (Allium sativum L.) over time.
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Garlic is a valuable source of healthy compounds, including secondary metabolites rich in sulphur such as cysteine sulphoxides (CSOs). Here, we present new qRT-PCR assays analysing the transcription of two genes encoding key enzymes in CSO biosynthetic pathways (cysteine synthase and alliinase) in
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