arachis villosa/protease

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Targeted expression of a cysteine protease (AdCP) in tapetum induces male sterility in Indian mustard, Brassica juncea.

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The development of male sterile plants is a prerequisite to developing hybrid varieties to harness the benefits of hybrid vigor in crops and enhancing crop productivity for sustainable agriculture. In plants, cysteine proteases have been known for their multifaceted roles during programmed cell

The structure of Bowman-Birk type protease inhibitor A-II from peanut (Arachis hypogaea) at 3.3 A resolution.

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The structure of Bowman-Birk type protease inhibitor (A-II from peanut) is described at 3.3 A resolution. The molecules form a tetramer with 222 local symmetry in our crystals. Each monomer has an elongated shape with approximate dimensions of 45 X 15 X 15 A and consists of two distinct domains. The

Crystallographic refinement of Bowman-Birk type protease inhibitor A-II from peanut (Arachis hypogaea) at 2.3 A resolution.

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The crystal structure of Bowman-Birk type protease inhibitor A-II from peanut was refined at 2.3 A resolution using a restrained least-squares method. The crystallographic R-factor is 0.196 for 7697 reflections with F > 3 sigma (F) in the range from 6.0 to 2.3 A resolution. Two molecules in an

Crystallization of Bowman-Birk type protease inhibitor (peanut) and its complex with trypsin.

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Crystallization and preliminary crystallographic study of Bowman-Birk type protease inhibitors, A-I, A-II, and B-III from peanut seeds (Arachis hypogaea), and of the A-II + trypsin complex were carried out. A-II, with 70 amino acid residues, crystallizes in a trigonal system, P3(1)21 (or P3(2)21), a

Purification and characterization of protease inhibitors from peanuts (Arachis hypogaea).

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Five protease inhibitors were isolated from peanut seeds and named A-I, A-II, B-I, B-II, and B-III. These inhibitors seemed to be Bowman-Birk type inhibitors judging from their low molecular weights and high cystine contents. All the inhibitors inhibited both bovine trypsin and chymotrypsin at

Expression of a pathogen-induced cysteine protease (AdCP) in tapetum results in male sterility in transgenic tobacco.

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Usable male sterility systems have immense potential in developing hybrid varieties in crop plants, which can also be used as a biological safety containment to prevent horizontal transgene flow. Barnase-Barstar system developed earlier was the first approach to engineer male sterility in plants. In

Targeted expression of cystatin restores fertility in cysteine protease induced male sterile tobacco plants.

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Fertility restoration in male sterile plants is an essential requirement for their utilization in hybrid seed production. In an earlier investigation, we have demonstrated that the targeted expression of a cysteine protease in tapetal cell layer resulted in complete male sterility in tobacco

[On plant protease inhibitors. VI. Purification of polyvalent protease inhibitors from Arachis hypogaea].

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Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions.

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Resistance to proteolytic enzymes and heat is thought to be a prerequisite property of food allergens. Allergens from peanut (Arachis hypogaea) are the most frequent cause of fatal food allergic reactions. The allergenic 2S albumin Ara h 2 and the homologous minor allergen Ara h 6 were studied at

Characterization of a vacuolar processing enzyme expressed in Arachis diogoi in resistance responses against late leaf spot pathogen, Phaeoisariopsis personata.

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Vacuolar processing enzymes are cysteine proteases responsible for maturation of vacuolar proteins. They have been shown to possess caspase-1-like activity, mediate cell death and display increased activity during pathogen infections. A transcript derived fragment corresponding to VPE was found to

Evaluating pH-induced gastrointestinal aggregation of Arachis hypogaea 1 fragments as potential components of peanut allergy.

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The seed storage glycoprotein Arachis hypogaea (Ara h) 1 is a major allergen found in peanuts. The biochemical resistance of food proteins to protease digestion contributes to their allergenicity. The rapid proteolysis of Ara h 1 under gastric conditions challenges this model. Biophysical and in

Some 2S albumin from peanut seeds exhibits inhibitory activity against Aspergillus flavus.

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A crude 2S albumin fraction was separated from peanut (Arachis hypogaea L.) cotyledons. Untreated 2S albumin had little inhibitory activity against trypsin, spore germination, or hyphal growth of Aspergillus flavus. However, following treatment of 2S albumin with SDS, increased inhibitory activity

Amino acid sequences of trypsin-chymotrypsin inhibitors (A-I, A-II, B-I, and B-II) from peanut (Arachis hypogaea): a discussion on the molecular evolution of legume Bowman-Birk type inhibitors.

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The amino acid sequences of four peanut protease inhibitors (A-I, A-II, B-I, and B-II) were determined by conventional methods and by comparison of peptide maps of their tryptic digests with that of B-III on HPLC. A-I, A-II, B-I, and B-III had the same amino acid sequence except for differences in

Amino acid sequence of a trypsin-chymotrypsin inhibitor, B-III, of peanut (Arachis hypogaea).

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The amino acid sequence of peanut trypsin-chymotrypsin inhibitor, B-III, was determined by conventional methods. The limited proteolysis of B-III with trypsin indicated the reactive sites of B-III for trypsin to be Arg(10)-Arg(11) and Arg(38)-Ser(39). Comparison of the established sequence of B-III

The 2S albumin allergens of Arachis hypogaea, Ara h 2 and Ara h 6, are the major elicitors of anaphylaxis and can effectively desensitize peanut-allergic mice.

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BACKGROUND Ara h 2 and Ara h 6, co-purified together in a 13-25 kD fraction (Ara h 2/6; 20 kD fraction) on gel filtration chromatography, account for the majority of effector activity in a crude peanut extract (CPE) when assayed with RBL SX-38 cells sensitized with IgE from human peanut allergic

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