avena/protease

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Ukurasa 1 kutoka 28 matokeo

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

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Ingia / Ingia

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.

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

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Ingia / Ingia

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

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

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Ingia / Ingia

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

Effects of exogenous 1,3-diaminopropane and spermidine on senescence of oat leaves : I. Inhibition of protease activity, ethylene production, and chlorophyll loss as related to polyamine content.

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Ingia / Ingia

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

Plant seed protease inhibitors differentially affect innate immunity in a tumor microenvironment to control hepatocarcinoma.

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Ingia / Ingia

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

Purification and characterization of serine proteases that exhibit caspase-like activity and are associated with programmed cell death in Avena sativa.

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Ingia / Ingia

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

Purification and properties of aminoaldehyde dehydrogenase from Avena sativa.

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Ingia / Ingia

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

Spectral Characterization and Proteolytic Mapping of Native 120-Kilodalton Phytochrome from Cucurbita pepo L.

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Ingia / Ingia

A spectral, immunochemical, and proteolytic characterization of native 120-kilodalton (kD) phytochrome from Cucurbita pepo L. is presented and compared with that previously reported for native 124-kD phytochrome from Avena sativa. The molecule was partially purified ( approximately 200-fold) in the

Hemin inhibits ubiquitin-dependent proteolysis in both a higher plant and yeast.

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Ingia / Ingia

In eukaryotes, a major route for ATP-dependent protein breakdown proceeds through covalent intermediates of target proteins destined for degradation and the highly conserved, 76 amino acid protein ubiquitin. In rabbit reticulocytes, it has been shown that hemin effectively inhibits this pathway by

The dark reactions of rye phytochrome in vivo and in vitro.

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Ingia / Ingia

The dark reactions of Secale cereale L. cv. Balbo phytochrome have been investigated in coleoptile tips and in extensively purified extracts of large molecular weight phytochrome. Destruction, but not reversion, was detected in vivo. The effects of various inhibitors of an in vitro

TLC-Bioautography as a fast and cheap screening method for the detection of α-chymotrypsin inhibitors in crude plant extracts.

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Ingia / Ingia

TLC-Bioautography is a fast and effective method for assessing the inhibitory effect of compounds present in plant extracts against microbial species. However, this method has a hidden, currently underutilized potential for evaluating the presence of inhibitory compounds against selected enzymes.

Purification of oat and rye phytochrome.

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Ingia / Ingia

A purification procedure employing normal chromatographic techniques is outlined for isolating phytochrome from etiolated oat (Avena sativa L.) seedlings. Yields in excess of 20% (25 milligrams or more) of phytochrome in crude extract were obtained from 10- to 15-kilograms lots. The purified oat

Purification and properties of betaine aldehyde dehydrogenase from Avena sativa.

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Ingia / Ingia

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

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

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Ingia / Ingia

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,

Proteolysis of endogenous substrates in senescing oat leaves : I. Specific degradation of ribulose bisphosphate carboxylase.

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Ingia / Ingia

Proteolysis of ribulose bisphosphate carboxylase (RuBPCase) during senescence was monitored using oat leaf segments (Avena sativa cv Victory), kept in the dark. We here report the development of a novel approach for measuring protein degradation of endogenous substrates both in situ and in vitro in

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