cucurbita palmata/protease

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Location of caspase 3-like protease in the development of sieve element and tracheary element of stem in Cucurbita moschata.

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The casepase is considered to regulate the process of programmed cell death in the development of organisms. In this study, caspase 3-like protease was detected by immunohistochemistry and immunoelectron microscopy during the development of sieve element and tracheary element of stem in Cucurbita

Hydrolysis with Cucurbita ficifolia serine protease reduces antigenic response to bovine whey protein concentrate and αs-casein.

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In the present study the effect of hydrolysis with non-commercial Cucurbita ficifolia serine protease on a reduction of the IgE and IgG binding capacity of whey protein concentrate and αs-casein was investigated. The intensity of the protein degradation was analyzed by the degree of hydrolysis, the

The Evaluation of Dipeptidyl Peptidase (DPP)-IV, α-Glucosidase and Angiotensin Converting Enzyme (ACE) Inhibitory Activities of Whey Proteins Hydrolyzed with Serine Protease Isolated from Asian Pumpkin (Cucurbita ficifolia).

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In the present study, whey protein concentrate (WPC-80) and β-lactoglobulin were hydrolyzed with a noncommercial serine protease isolated from Asian pumpkin (Cucurbita ficifolia). Hydrolysates were further fractionated by ultrafiltration using membranes with cut-offs equal 3 and 10 kDa. Peptide

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

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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

Optimization of preparation of antioxidative peptides from pumpkin seeds using response surface method.

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Protein isolates of pumpkin (Cucurbita pepo L) seeds were hydrolyzed by acid protease to prepare antioxidative peptides. The hydrolysis conditions were optimized through Box-Behnken experimental design combined with response surface method (RSM). The second-order model, developed for the DPPH

A reinvestigation on the quaternary structure of ascorbate oxidase from Cucurbita pepo medullosa.

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The optical properties, copper content, catalytic activity and quaternary structure of many preparations of ascorbate oxidase purified with two different methods were examined. Fresh samples appeared identical and were characterized by optical ratios A280/A610 = 25 +/- 1 and A330/A610 = 0.8 +/-

Selenium species determination in selenium-enriched pumpkin (Cucurbita pepo L.) seeds by HPLC-UV-HG-AFS.

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Pumpkins were treated by spraying the leaves in the flowering period with a water solution containing 1.5 mg Se per liter in the form of Na2SeO4. The average total selenium content of seeds was found to be 0.19 microg g(-1) in nontreated pumpkins and 1.1 microg g(-1) in exposed ones. For speciation

Detection and in vitro studies of Cucurbita maxima phloem serpin-1 RNA-binding properties.

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Apart from being a conduit for photoassimilate transport in plants, the phloem serves as a pathway for transport of proteins and RNAs from sites of their synthesis to distant plant parts. As demonstrated for mRNAs and small RNAs such as miRNA and siRNA, their phloem transport is largely involved in

Differential modulation of binding loop flexibility and stability by Arg50 and Arg52 in Cucurbita maxima trypsin inhibitor-V deduced by trypsin-catalyzed hydrolysis and NMR spectroscopy.

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The side chains of Arg50 and Arg52 iin Cucurbita maxima trypsin inhibitor-V (CMTI-V) anchor the binding loop to the scaffold region [Cai, M., Gong, Y., Kao, J.L-F., & Krishnamoorthi, R. (1995) Biochemistry 34, 5201-5211]. The consequences of these hydrogen-bonding and electrostatic interactions on

A new protein inhibitor of trypsin and activated Hageman factor from pumpkin (Cucurbita maxima) seeds.

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A protein inhibitor (CMTI-V; Mr 7106) of trypsin and activated Hageman factor (Factor XIIa), a serine protease involved in blood coagulation, has been isolated for the first time from pumpkin (Cucurbita maxima) seeds by means of trypsin-affinity chromatography and reverse phase high performance

Protein transport into higher plant peroxisomes. In vitro import assay provides evidence for receptor involvement.

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Peroxisome biogenesis requires that proteins be transported from their site of synthesis in the cytoplasm to their final location in the peroxisome matrix or membrane. Glyoxysomes are a class of peroxisomes found primarily in germinating seedlings and are involved in mobilizing fatty acids via the

High-resolution structures of three new trypsin-squash-inhibitor complexes: a detailed comparison with other trypsins and their complexes.

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An anionic trypsin from Atlantic salmon and bovine trypsin have been complexed with the squash-seed inhibitors, CMTI-I (Cucurbita maxima trypsin inhibitor I, P1 Arg) and CPTI-II (Cucurbita pepo trypsin inhibitor II, P1 Lys). The crystal structures of three such complexes have been determined to

Zucchini yellow mosaic virus: insect transmission and pathogenicity -the tails of two proteins.

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SUMMARY Taxonomy: Zucchini yellow mosaic virus (ZYMV) is a member of genus Potyvirus, family Potyviridae. ZYMV is a positive-strand RNA virus. Physical properties: Virions are flexuous filaments of 680-730 nm in length and 11-13 nm in diameter, composed of about 2000 subunits of a single 31-kDa

Native phytochrome: immunoblot analysis of relative molecular mass and in-vitro proteolytic degradation for several plant species.

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The relative molecular mass (Mr) of the native phytochrome monomer from etiolated Cucurbita pepo L., Pisum sativum L., Secale cereale L. and Zea mays L. seedlings has been determined using immunoblotting to visualize the chromoprotein in crude extracts subjected to sodium dodecyl

Cytoplasmic Orientation of the Naphthylphthalamic Acid-Binding Protein in Zucchini Plasma Membrane Vesicles.

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Polar transport of the plant hormone auxin is blocked by substances such as N-1-naphthylphthalamic acid (NPA), which inhibit auxin efflux and block polar auxin transport. To understand how auxin transport is regulated in vivo, it is necessary to discern whether auxin transport inhibitors act at the

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