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clitoria falcata/carbohydrate

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Compact acid-induced state of Clitoria ternatea agglutinin retains its biological activity.

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The effects of pH on Clitoria ternatea agglutinin (CTA) were studied by spectroscopy, size-exclusion chromatography, and by measuring carbohydrate specificity. At pH 2.6, CTA lacks well-defined tertiary structure, as seen by fluorescence and near-UV CD spectra. Far-UV CD spectra show retention of

Purification and characterization of a novel beta-D-galactosides-specific lectin from Clitoria ternatea.

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A lectin present in seeds of Clitoria ternatea agglutinated trypsin-treated human B erythrocytes. The sugar specificity assay indicated that lectin belongs to Gal/Gal NAc-specific group. Hence the lectin, designated C. ternatea agglutinin (CTA), was purified by the combination of acetic acid

Antinociceptive and anti-inflammatory effects of a lectin-like substance from Clitoria fairchildiana R. Howard seeds.

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Lectins are proteins that have the ability to bind specifically and reversibly to carbohydrates and glycoconjugates, without altering the structure of the glycosyl ligand. They are found in organisms such as viruses, plants and humans, and they have been shown to possess important biological
Screening of natural products for mosquito larvicidal activity against three major mosquito vectors Aedes aegypti, Culex quinquefasciatus, and Anopheles stephensi resulted in the identification of three potential plant extracts viz., Saraca indica/asoca, Nyctanthes arbor-tristis, and Clitoria
This study aimed to assess the effect of the Clitoria ternatea L. flower extract (CTE), on the inhibition of pancreatic α-amylase, in vitro starch hydrolysis, and predicted the glycemic index of different type of flours including potato, cassava, rice, corn, wheat, and glutinous rice flour. The
BACKGROUND Plant-based foods have been used in traditional health systems to treat diabetes mellitus. The successful prevention of the onset of diabetes consists in controlling postprandial hyperglycemia by the inhibition of α-glucosidase and pancreatic α-amylase activities, resulting in aggressive
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