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crotalaria cobalticola/cysteine

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5 results

Increase of free cysteine and citric acid in plant cells exposed to cobalt ions.

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Cobalt complexation was investigated in a suspension cell culture of the cobalt hyperaccumulator Crotalaria cobalticola. C. cobalticola cells were more tolerant towards cobalt ions than the suspension cells of the non-accumulators Rauvolfia serpentina and Silene cucubalus. While the concentration of

Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly).

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A proteinaceous trypsin inhibitor was purified from Crotalaria pallida seeds by ammonium sulfate precipitation, affinity chromatography on immobilized trypsin-Sepharose and TCA precipitation. The trypsin inhibitor, named CpaTI, had M(r) of 32.5 kDa as determined by SDS-PAGE and was composed of two

Lectin, hemolysin and protease inhibitors in seed fractions with ovicidal activity against Haemonchus contortus.

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Bioactive molecules of plant species are promising alternatives for the chemical control of gastrointestinal nematodes in ruminants. Extracts of native and exotic seed species from Brazil's semi-arid region were tested in vitro in an egg hatch assay and the bioactivity of their proteins was

Study of the proteolytic activity of the tropical legume Crotalaria spectabilis.

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The characterization of legume proteases contributes to the understanding of the physiology of plants and their interaction with the environment. Thirteen extracts from various parts of Crotalaria spectabilis were made using different extraction systems. The highest protein content was found in

Chemical modification studies on a blood group A-specific lectin, crotalarin (Crotalaria striata) and its effect on hemagglutinating activity.

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Crotalarin, the N-acetyl-D-galactosamine-binding blood group A-specific lectin from the seeds of Crotalaria striata was subjected to various chemical modifications in order to ascertain the amino acid residues responsible for its carbohydrate-binding property. Modification of lysine, cysteine and
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