phaseolus parvulus/antifungic

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Lunatin, a novel lectin with antifungal and antiproliferative bioactivities from Phaseolus lunatus billb.

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A novel lectin with a molecular mass of 24.3kDa, designated Lunatin, was isolated from edible seeds of Phaseolus lunatus billb. The purification scheme consisted of ammonium sulfate precipitation, affinity chromatography, ion exchange chromatography, and gel filtration chromatography. The lectin is

A leguminous trypsin-chymotrypsin inhibitor Limenin with antifungal activity from Phaseolus limensis.

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A trypsin-chymotrypsin inhibitor, designated Limenin, with both antifungal and antibacterial activity, and exhibiting a molecular mass of 18.0 kDa in SDS-polyacrylamide gel electrophoresis, was isolated from the large lima bean (Phaseolus limensis) legumes by a combination of

An antifungal peptide from Phaseolus vulgaris cv. brown kidney bean.

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A 5.4-kDa antifungal peptide, with an N-terminal sequence highly homologous to defensins and inhibitory activity against Mycosphaerella arachidicola (IC(50)= 3 μM), Setospaeria turcica and Bipolaris maydis, was isolated from the seeds of Phaseolus vulgaris cv. brown kidney bean. The peptide was

Vulgarinin, a broad-spectrum antifungal peptide from haricot beans (Phaseolus vulgaris).

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From the seeds of haricot beans (Phaseolus vulgaris), an antifungal peptide with a molecular mass around 7 kDa was purified by using a simple protocol consisting of affinity chromatography on Affi-gel blue gel and gel filtration on Superdex 75. This peptide named vulgarinin manifested an antifungal

An antifungal peptide from baby lima bean.

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A 6-kDa antifungal peptide with inhibitory activity on mycelial growth in Fusarium oxysporum, Mycosphaerella arachidicola, and Physalospora piricola was isolated from baby lima beans. The peptide suppressed growth in M. arachidicola with an IC(50) of 0.87 muM and inhibited activity of HIV-1 reverse

Phaseococcin, an antifungal protein with antiproliferative and anti-HIV-1 reverse transcriptase activities from small scarlet runner beans.

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From the seeds of small scarlet runner beans (Phaseolus coccineus 'Minor'), an antifungal protein with an N-terminal sequence homologous to those of defensins was isolated. The antifungal protein bound to Affi-gel blue gel and Mono S but it did not bind to DEAE-cellulose. It was further purified by

Coccinin, an antifungal peptide with antiproliferative and HIV-1 reverse transcriptase inhibitory activities from large scarlet runner beans.

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An antifungal peptide, designated coccinin, with a molecular mass of 7kDa and an N-terminal sequence resembling those of defensins, was purified from the seeds of large scarlet runner beans (Phaseolus coccineus cv. 'Major'). The peptide isolated was unadsorbed on DEAE-cellulose, and adsorbed on

Isolation and biochemical characterization of a novel leguminous defense peptide with antifungal and antiproliferative potency.

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Leguminous plants have formed a popular subject of research owing to the abundance of proteins and peptides with important biological activities that they produce. The antifungal proteins and peptides have been purified from a number of leguminous species. However, research continues to discover

Investigations on fungicides. XVI. Natural resistance of plant roots to fungal pathogens.

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Uninoculated roots of pea (Pisum sativum) and French bean (Phaseolus vulgaris) have been shown to exude a number of antifungal compounds when grown in a non-sterile aqueous aerated medium. These have been identified and their possible importance in relation to disease resistance is discussed.

Biochemical and biophysical changes induced by fungicide sodium diethyl dithiocarbamate (SDD), in phytocystatin purified from Phaseolus mungo (Urd): a commonly used Indian legume.

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Phytocystatins are the plant thiol protease inhibitors involved in several reaction mechanisms of the plant system like regulation of proteolytic activity and storage of proteins. Biochemical and biophysical changes induced by fungicide SDD in phytocystatin purified from Phaseolus mungo have been

Concurrent isolation of a Kunitz-type trypsin inhibitor with antifungal activity and a novel lectin from Pseudostellaria heterophylla roots.

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A simple purification protocol, involving ion exchange chromatography on DEAE-cellulose and CM-cellulose and fast protein liquid chromatography-gel filtration on Superdex 75, was employed to isolate a Kunitz-type trypsin inhibitor with antifungal activity and a novel lectin from Pseudostellaria

Baseline and Differential Sensitivity to Two QoI Fungicides Among Isolates of Phytophthora cactorum That Cause Leather Rot and Crown Rot on Strawberry.

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Sensitivities of 89 isolates of Phytophthora cactorum, the causal agent of crown rot and leather rot on strawberry plants, from seven states (Florida, Maine, North Carolina, Ohio, Oregon, South Carolina, and New York) to the QoI fungicide azoxystrobin were determined based on mycelium growth and

Northeast red beans produce a thermostable and pH-stable defensin-like peptide with potent antifungal activity.

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A 5.4-kDa antifungal peptide was purified from Phaseolus vulgaris L. cv. "northeast red bean" using a protocol that entailed affinity chromatography, ion exchange chromatography, and gel filtration. The molecular mass was determined by matrix-assisted laser desorption ionization time-of-flight. The

Isolation of a thermostable legume chitinase and study on the antifungal activity.

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Chitinases are listed as one class of pathogenesis-related proteins, and they have become a popular research topic because of their resistance to plant-pathogenic diseases. A chitinase with antifungal activity was isolated from the Canadian cranberry beans (Phaseolus vulgaris). The procedure

Concurrent purification of two defense proteins from French bean seeds: a defensin-like antifungal peptide and a hemagglutinin.

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A purification protocol is described herein for concurrent isolation of two defense proteins including a 6-kDa defensin-like antifungal peptide and a 60-kDa dimeric hemagglutinin from seeds of the French bean (Phaseolus vulgaris). It involved ion-exchange chromatography on SP-Sepharose, affinity

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