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avena/protease

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ArtiklidKliinilistes uuringutesPatendid
Leht 1 alates 33 tulemused

beta-d-Glucan of Avena Coleoptile Cell Walls.

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A specific glucanase was used to liberate a noncellulosic beta-d-glucan from isolated cell walls of Avena sativa coleoptile tissue. Cell walls of this tissue contain as much as 7 to 9 mg of glucan/100 mg of dry wall. Because of the specific action pattern of the enzyme, a linkage sequence of.. 1 -->

Purification and properties of aminoaldehyde dehydrogenase from Avena sativa.

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NAD-dependent aminoaldehyde dehydrogenase (AMADH, EC 1.2.1.-) from Avena shoots was purified by DEAE Sephacel, hydroxyapatite, 5'-AMP Sepharose 4B, Mono Q, and TSK-GEL column chromatographies to homogeneity by the criterion of native PAGE. SDS-PAGE yielded a single band at a molecular mass of 55

Subcellular Localization of Proteases in Developing Leaves of Oats (Avena sativa L.).

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The distribution and subcellular localization of the two major proteases present in oat (Avena sativa L. cv Victory) leaves was investigated. Both the acidic protease, active at pH 4.5, and the neutral protease, active at pH 7.5, are soluble enzymes; a few percent of the enzyme activity was

Purification and properties of betaine aldehyde dehydrogenase from Avena sativa.

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Betaine aldehyde dehydrogenase (BADH; EC 1.2.1.8) is the enzyme that catalyzes the second step in the synthesis of the osmoprotectant, glycine betaine. NAD-dependent BADH was purified from Avena sativa shoots by DEAE Sephacel, hydroxyapatite, 5'-AMP Sepharose 4B, Mono Q and TSK-GEL column

Proteolysis alters the spectral properties of 124 kdalton phytochrome from Avena.

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Native phytochrome from Avena sativa L. is homogeneous with a monomeric molecular weight of 124 kdalton; 6-10 kdalton larger than the heterogeneous "120" kdalton preparations previously considered to be undegraded (Vierstra and Quail, 1982, Proc. Natl. Acad. Sci. USA, 79: 5272-5276). The

Spectral perturbations and oligomer/monomer formation in 124-kilodalton Avena phytochrome.

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We have studied the effects of pH, ionic strength, and hydrophobic fluorescence probes, 8-anilinonaphthalene-1-sulfonate (ANS) and bis-ANS, on the structure of intact (124-kDa) Avena phytochrome. The Pfr form of phytochrome forms oligomers in solution to a greater extent than the Pr form.

Purification and initial characterization of ubiquitin from the higher plant, Avena sativa.

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Ubiquitin is a highly conserved, 76-amino acid polypeptide recently demonstrated to be involved in ATP-dependent protein degradation in mammalian cells. From immunoblot analyses with anti-human-ubiquitin antibodies we have detected the presence of free ubiquitin in green leaves, etiolated shoots,

Expression of AP 3, 4 and 5 isophytochromes in etiolated oat seedlings (Avena sativa L.).

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Type 1 phytochrome from etiolated oat seedlings was digested with V-8 protease. Microsequencing of a 13 kDa fragment yielded a sequence of 31 amino acids. The fragment starting with the alanine residue at position 427 of the entire phytochrome amino acid sequence revealed a heterogeneity (threonine,
Victoria blight of Avena sativa (oat) is caused by the fungus Cochliobolus victoriae, which is pathogenic because of the production of the toxin victorin. The victorin-induced response in sensitive A. sativa has been characterized as a form of programmed cell death (PCD) and displays morphological

The role of separate molecular domains in the structure of phytochrome from etiolated Avena sativa L.

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The spectral properties of peptides generated from etiolated-Avana, 124-kDa (kilodalton) phytochrome by endogenous protease(s) have been studied to assess the role of the amino-terminal and the carboxyl-terminal domains in maintaining the proper interaction between protein and chromophore. The
The renin-angiotensin-aldosterone system (RAAS) plays an important role in regulating hypertension by controlling vasoconstriction and intravascular fluid volume. RAAS itself is largely regulated by the actions of renin (EC 3.4.23.15) and the angiotensin-I-converting enzyme (ACE-I; EC 3.4.15.1). The

Proteases of senescing oat leaves: I. Purification and general properties.

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Two proteases active in the senescing first leaves of oat seedlings (Avena sativa cv. Victory) have been purified approximately 500-fold by a combination of ammonium sulfate precipitation, affinity chromatography on hemoglobin-Sepharose, and ion exchange chromatography on DEAE-Sephadex. The enzymes

Proteases of Senescing Oat Leaves: II. Reaction to Substrates and Inhibitors.

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Two proteases isolated from senescent oat (Avena sativa) leaves have been subjected to further study. One of these, an acid protease active at pH 4.2, is inhibited by phenylmethylsulfonyl fluoride (PMSF) but not by iodoacetamide (IAc). The other, active at pH 6.6, is inhibited by both PMSF and IAc.
Excision and dark incubation of oat (Avena sativa L., var. Victory) leaves cause a sharp increase in protease activity, which precedes Chl loss. Both these senescence processes are inhibited by exogenously applied 1,3-diaminopropane (Dap), which occurs naturally in leaf segments. The inhibition of
Identifying tolerance responses to ingested foodstuff over life is essential for understanding dysfunction in metabolic diseases. This study presents a comparative structural and functional analysis of serine-type protease inhibitors (STPIs) from Chenopodium quinoa, Salvia hispanica L., Avena sativa
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