senna occidentalis/protease

Sábháiltear an nasc chuig an gearrthaisce

AiltTrialacha cliniciúlaPaitinní

Roghnaigh cineál sórtála

9 torthaí

A study on trypsin, Aspergillus flavus and Bacillus sp. protease inhibitory activity in Cassia tora (L.) syn Senna tora (L.) Roxb. seed extract.

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Logáil Isteach / Cláraigh

BACKGROUND Proteases play an important role in virulence of many human, plant and insect pathogens. The proteinaceous protease inhibitors of plant origin have been reported widely from many plant species. The inhibitors may potentially be used for multiple therapeutic applications in viral,

Local and systemic toxicity of Echis carinatus venom: neutralization by Cassia auriculata L. leaf methanol extract.

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Logáil Isteach / Cláraigh

Viper bites cause high morbidity and mortality especially in tropical and subtropical regions, affecting a large number of the rural population in these areas. Even though anti-venoms are available, in most cases they fail to tackle viper venom-induced local manifestations that persist even after

Comparative transcriptome analysis provides insights of anti-insect molecular mechanism of Cassia obtusifolia trypsin inhibitor against Pieris rapae.

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Logáil Isteach / Cláraigh

Pieris rapae, a serious Lepidoptera pest of cultivated crucifers, utilizes midgut enzymes to digest food and detoxify secondary metabolites from host plants. A recombinant trypsin inhibitor (COTI) from nonhost plant, Cassia obtusifolia, significantly decreased activities of trypsin-like proteases in

Assimilatory potential of Helicoverpa armigera reared on host (Chickpea) and nonhost (Cassia tora) diets.

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Logáil Isteach / Cláraigh

Adaptation to plant allelochemicals is a crucial aspect of herbivore chemical ecology. To understand an insect ecology, we studied an effect of nonhost Cassia tora seed-based diet (Ct) on growth, development, and molecular responses in Helicoverpa armigera. We employed a comparative approach to

Traditional Chinese medicine herbal extracts of Cibotium barometz, Gentiana scabra, Dioscorea batatas, Cassia tora, and Taxillus chinensis inhibit SARS-CoV replication.

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Logáil Isteach / Cláraigh

Development of anti-severe acute respiratory syndrome associated coronavirus (SARS-CoV) agents is pivotal to prevent the reemergence of the life-threatening disease, SARS. In this study, more than 200 extracts from Chinese medicinal herbs were evaluated for anti-SARS-CoV activities using a

Structural and functional relationship of Cassia obtusifolia trypsin inhibitor to understand its digestive resistance against Pieris rapae.

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Logáil Isteach / Cláraigh

Although digestive resistance of Kunitz protease inhibitors has been reported extensively, the molecular mechanism is not well established. In the present study, the first X-ray structure of Cassia obtusifolia trypsin inhibitor (COTI), a member of Kunitz protease inhibitors, was solved at a

Isolation, structure modeling and function characterization of a trypsin inhibitor from Cassia obtusifolia.

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Logáil Isteach / Cláraigh

A trypsin inhibitor gene (CoTI1) from Cassia obtusifolia was isolated and the deduced amino acid sequence was attributed to the Kunitz-type trypsin inhibitor. The recombined CoTI1, expressed in E. coli, exhibited strong inhibitory effect on bovine trypsin and trypsin-like proteases from Helicoverpa

Composition, characteristics, and in-vitro physiological effects of the water-soluble polysaccharides from Cassia seed.

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Logáil Isteach / Cláraigh

The popular beverage ingredients Cassia obtusifolia and Cassia tora were found to have considerable amounts of water-soluble polysaccharides (WSPs) (58.5 and 55.9/100g of dried extract). The composition, characteristics, and in-vitro physiological effects of these polysaccharides and their possible

A trypsin inhibitor from Cassia obtusifolia seeds: isolation, characterization and activity against Pieris rapae.

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Logáil Isteach / Cláraigh

A trypsin inhibitor was isolated from Cassia obtusifolia by ammonium sulfate precipitation, Sepharose 4B-trypsin affinity and Sephadex G-75 chromatography. The inhibitor consisted of a single polypeptide chain with a molecular mass of 19, 812.55 Da. It was stable from pH 2 to 12 for 24 h, whereas it

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