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artocarpus chaplasha/protease

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Antimicrobial activity of a 48-kDa protease (AMP48) from Artocarpus heterophyllus latex.

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OBJECTIVE Artocarpus heterophyllus (jackfruit) is a latex producing plant. Plant latex is produced from secretory cells and contains many intergradients. It also has been used in folk medicine. This study aimed to purify and characterize the biological activities of a protease from jackfruit
Pharmacological properties exhibited by latex of plants are due to various biologically active compounds including several proteolytic enzymes. Present study evaluates hemostatic potential of Tabernaemontana divaricata and Artocarpus altilis from Apocynaceae and Moraceae families respectively. The

A novel serine protease with human fibrino(geno)lytic activities from Artocarpus heterophyllus latex.

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A protease was isolated and purified from Artocarpus heterophyllus (jackfruit) latex and designated as a 48-kDa antimicrobial protease (AMP48) in a previous publication. In this work, the enzyme was characterized for more biochemical and medicinal properties. Enzyme activity of AMP48 was strongly
Plant latex has many health benefits and has been used in folk medicine. In this study, the biological effect of Artocarpus heterophyllus (jackfruit) latex on human blood coagulation was investigated. By a combination of heat precipitation and ion-exchange chromatography, a heat stable

Studies on the specificity of the IgA-binding lectin, jacalin.

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The interactions of IgA with the jackfruit lectin, jacalin, were investigated with regard to the specificity of jacalin for species and subclasses of IgA. It was found that jacalin selectively bound to human IgA1, but not to human IgA2, mouse IgA or rat IgA. Binding studies with human IgA1 fragments

New geranyl flavonoids from the leaves of Artocarpus communis.

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Four new geranyl flavonoids 1-4 and four known flavonoids 5-8 were obtained from the leaves of Artocarpus communis collected in Indonesia. The planar structures of flavonoids were elucidated by analyses of MS and NMR spectroscopic data. Absolute configurations of 1 and 2 were determined by ECD
Protein hydrolysates usually possess higher nutritive value than an equivalent mixture of free amino acids. This study was aimed at determining the antioxidant activities of protein hydrolysates of Treculia africana seeds. Soluble protein was isolated from Treculia africana seed flour
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