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hordeum distichon/l tyrosine

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Plant tyrosine decarboxylase can be strongly inhibited by L-α-aminooxy-β-phenylpropionate.

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Tyrosine decarboxylase (EC 4.1.1.25) from Syringa vulgaris L. cell cultures and from Hordeum vulgare L. seedlings is strongly inhibited by the phenylalanine analogue, L-α-aminooxy-β-phenylpropionate. L-α-Aminooxy-β-phenylpropionate is therefore not specific in its inhibitory action against
Chitinase isolated from Zea mays seeds is inactivated by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) in the absence of exogenous nucleophiles. Oligomers of N-acetylglucosamine,N,N',N",N"'-tetra-N-acetylchitotetraose (GlcNAc4), and to a lesser extent, N,N',N"-tri-N-acetylchitotriose (GlcNAc3)

A Proteinase from Germinated Barley : II. Hydrolytic Specificity of a 30 Kilodalton Cysteine Proteinase From Green Malt.

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The hydrolytic specificity of a 30 kilodalton cysteine proteinase purified from germinated barley (Hordeum vulgare L. cv Morex) was investigated using high performance liquid chromatography to characterize its hydrolysis of two small barley seed proteins, the alpha- and beta-hordothionins. The

Prediction of protein cleavage sites by the barley cysteine endoproteases EP-A and EP-B based on the kinetics of synthetic peptide hydrolysis.

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Hordeins, the natural substrates of barley (Hordeum vulgare) cysteine endoproteases (EPs), were isolated as protein bodies and degraded by purified EP-B from green barley malt. Cleavage specificity was determined by synthesizing internally quenched, fluorogenic tetrapeptide substrates of the general

Substrate specificity of barley cysteine endoproteases EP-A and EP-B.

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The cysteine endoproteases (EP)-A and EP-B were purified from green barley (Hordeum vulgare L.) malt, and their identity was confirmed by N-terminal amino acid sequencing. EP-B cleavage sites in recombinant type-C hordein were determined by N-terminal amino acid sequencing of the cleavage products,

Gramine attenuates EGFR-mediated inflammation and cell proliferation in oral carcinogenesis via regulation of NF-κB and STAT3 signaling.

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Gramine, a natural indole alkaloid found in Hordeum vulgare has been possesses anti-mutagenic properties. The aim of the present study was to evaluate the effect of gramine on inflammation and proliferation in 7,12-dimethylbenz[a]anthracene(DMBA)-induced hamster buccal pouch (HBP) carcinogenesis.

Physiological and biochemical response of soil-grown barley (Hordeum vulgare L.) to cerium oxide nanoparticles.

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A soil microcosm study was performed to examine the impacts of cerium oxide nanoparticles (nCeO2) on the physiology, productivity, and macromolecular composition of barley (Hordeum vulgare L.). The plants were cultivated in soil treated with nCeO2 at 0, 125, 250, and 500 mg kg(-1) (control, nCeO2-L,

Content analysis of vitamins, dietary fibers and amino acids in a wide collection of barley (Hordeum vulgare L.) from Tibet, China

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Barley (Hordeum vulgare L.) is an important agricultural crop. Various studies on the genetic diversity, biochemical and molecular attributes on this species are known. However, information on nutritional variability in a large panel of barley cultivars is limited. Therefore, it is of interest for a

Increasing sucrose uptake capacity of wheat grains stimulates storage protein synthesis.

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Increasing grain sink strength by improving assimilate uptake capacity could be a promising approach toward getting higher yield. The barley (Hordeum vulgare) sucrose transporter HvSUT1 (SUT) was expressed under control of the endosperm-specific Hordein B1 promoter (HO). Compared with the wild type,

Analysis of brome mosaic virus replication and aminoacylation functions by site-specific mutagenesis.

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Brome Mosaic Virus (BMV) has a tripartite RNA genome; each RNA and the subgenomic RNA encoding the viral coat protein share a highly homologous region of about 200 nucleotides at the 3' end, for which a tRNA-like structure has been proposed. Several sequences encoding functions, including replicase

Mode of action of the catalytic site in the N-terminal ribosome-inactivating domain of JIP60.

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Jasmonate-induced protein 60 (JIP60) is a ribosome-inactivating protein from barley (Hordeum vulgare) and is involved in the plant immune response dependent on the jasmonate hormones. Here, we demonstrate that transient expression in Nicotiana benthamiana of the N-terminal domain of JIP60, from

Identification of plastid envelope proteins required for import of protochlorophyllide oxidoreductase A into the chloroplast of barley.

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Chloroplasts synthesize an abundance of different tetrapyrrole compounds. Among them are chlorophyll and its precursor protochlorophyllide (Pchlide), which accumulate in light- and dark-grown plants, respectively. Pchlide is converted to chlorophyllide by virtue of the NADPH:Pchlide oxidoreductase

Studies on the release of barley aleurone cell proteins: Kinetics of labelling.

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Protein release from gibberellic acid-treated aleurone cells of barley (Hordeum vulgare L.) was followed in pulse-chase experiments with radioactively labelled amino acids. After a 10-min pulse of [(3)H]leucine or [(3)H]tryptophan, label was incorporated into trichloroacetic-acid (TCA)-insoluble

Enhanced green fluorescence by the expression of an Aequorea victoria green fluorescent protein mutant in mono- and dicotyledonous plant cells.

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The expression of the jellyfish green fluorescent protein (GFP) in plants was analyzed by transient expression in protoplasts from Nicotiana tabacum, Arabidopsis thaliana, Hordeum vulgare, and Zea mays. Expression of GFP was only observed with a mutated cDNA, from which a recently described cryptic
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