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cajanus cajan/protease
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10 Ergebnisse
Purification and Partial Characterization of Trypsin-Specific Proteinase Inhibitors from Pigeonpea Wild Relative Cajanus platycarpus L. (Fabaceae) Active against Gut Proteases of Lepidopteran Pest Helicoverpa armigera.
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Proteinase inhibitors (PIs) are natural defense proteins of plants found to be active against gut proteases of various insects. A pigeonpea wild relative Cajanus platycarpus was identified as a source of resistance against Helicoverpa armigera, a most devastating pest of several crops including
In vivo inhibition of Helicoverpa armigera gut pro-proteinase activation by non-host plant protease inhibitors.
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We evaluated 22 different host and non-host plant protease inhibitors (PIs) for in vivo inhibition of Helicoverpa armigera gut pro- and proteinases, and their biological activity against the pod borer, H. armigera, the most important pest of agriculture and horticultural crops worldwide. In vitro
Structural and Biophysical Characterization of Cajanus cajan Protease Inhibitor.
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BACKGROUND
A large number of studies have proven that Protease inhibitors (PIs), specifically serine protease inhibitors, show immense divergence in regulation of proteolysis by targeting their specific proteases and hence, they play a key role in healthcare.
OBJECTIVE
We aimed to access in-vitro
Effect of detergents and hexafluoroisopropanol on the conformation of a non-helical and a helical plant protease inhibitor.
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We have earlier reported the purification of a non-helical proteinase inhibitor from Cajanus cajan and a helical proteinase/amylase inhibitor from Phaseolus aureus. The effect of detergents, viz. sodium dodecyl sulfate (SDS), sodium deoxycholate (DOC) and 3-[(3-cholamidopropy)
Amylase inhibitors of pigeonpea (Cajanus cajan) seeds.
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Pigeonpea (Cajanus cajan L) seeds were analysed quantitatively for amylase inhibitor (AI) activity and qualitatively, by an in-gel-detection method on polyacrylamide gels. At least four AI isoforms were identified in pigeonpea seeds. The AIs inhibit human salivary and bovine pancreatic amylase but
Purification and characterization of a 43 kD hepatoprotective protein from the herb Cajanus indicus L.
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Cajanus indicus L, a herb, is popularly known for its hepatoprotective activity. Aqueous extract of the leaves of this plant contains hepatoprotective and hepatostimulatory molecule(s). Present study was aimed to isolate, purify and characterize the active principle(s) responsible for that activity.
Characterization of a proteinase inhibitor from Cajanus cajan (L.).
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A protein proteinase inhibitor (PI) has been purified from pigeonpea Cajanus cajan (L.) PUSA 33 variety by acetic-acid precipitation, salt fractionation and chromatography on a DEAE-Cellulose column. The content of inhibitor was found to be 15 mg/20 g dry weight of pulse. The molecular weight of the
Structural and functional characterization of proteinase inhibitors from seeds of Cajanus cajan (cv. ICP 7118).
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Proteinase inhibitors (C11PI) from mature dry seeds of Cajanus cajan (cv. ICP 7118) were purified by chromatography which resulted in 87-fold purification and 7.9% yield. SDS-PAGE, matrix assisted laser desorption ionization time-of-flight (MALDI-TOF/TOF) mass spectrum and two-dimensional (2-D) gel
Regulated partitioning of fixed carbon (14C), sodium (Na+), potassium (K+) and glycine betaine determined salinity stress tolerance of gamma irradiated pigeonpea [Cajanus cajan (L.) Millsp].
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Soil salinity is a major constraint that limits legume productivity. Pigeonpea is a salt sensitive crop. Seed gamma irradiation at a very low dose (2.5 Gy) is known to enhance seedling establishment, plant growth and yield of cereals and other crops. The present study conducted using two genetically
Trypsin Inhibitors from Cajanus cajan and Phaseolus limensis Possess Antioxidant, Anti-Inflammatory, and Antibacterial Activity.
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Protease inhibitors are one of the most promising and investigated subjects for their role in pharmacognostic and pharmacological studies. This study aimed to investigate antioxidant, anti-inflammatory, and antimicrobial activities of trypsin inhibitors (TIs) from two plant sources (Cajanus cajan
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