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momordica charantia lectin/momordica
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Momordica Charantia lectin, a type II ribosome inactivating protein, exhibits antitumor activity toward human nasopharyngeal carcinoma cells in vitro and in vivo.
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The incidence of nasopharyngeal carcinoma (NPC) remains high in endemic regions, including southern China, northern Africa, and North America. One of the promising therapeutic approaches on NPC is drug screening from natural products, such as components from traditional Chinese medicine. In this
Momordica charantia lectin exhibits antitumor activity towards hepatocellular carcinoma.
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BACKGROUND
The incidence and mortality of hepatocellular carcinoma (HCC) remain high worldwide. Drug screening from natural plants is one of the potential therapeutic approaches on HCC.
METHODS
The antitumor effect of momordica charantia lectin (MCL) was examined, using MTT, colony formation,
Toxicity of Momordica charantia lectin and inhibitor for human normal and leukaemic lymphocytes.
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A haemagglutinin (lectin) and another protein (inhibitor) purified from the seeds of Momordica charantia inhibited protein and subsequently DNA synthesis in normal (mitogen-stimulated) and leukaemic human peripheral blood lymphocytes. The effect of the lectin was more rapid and more pronounced than
Differential scanning calorimetric and spectroscopic studies on the unfolding of Momordica charantia lectin. Similar modes of thermal and chemical denaturation.
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Thermal stability of Momordica charantia seed lectin (MCL) was investigated as a function of protein concentration, pH, scan rate, and at different ligand concentrations by using high-sensitivity differential scanning calorimetry (DSC). The DSC endotherm obtained at pH 7.4 consists of two entities
Binding of 4-methylumbelliferyl beta-D-galactopyranoside to Momordica charantia lectin: fluorescence-quenching studies.
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The binding of 4-methylumbelliferyl beta-D-galactopyranoside (MeUmb-Galp), to Mormordica charantia lectin was studied by equilibrium dialysis and quenching of ligand fluorescence. The fluorescence of MeUmb-Galp decreases as a function of solvent polarity. On binding to M. charantia lectin, its
Isolation and partial characterization of 3 nontoxic d-galactose-specific isolectins from seeds of Momordica balsamina.
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Three isolectins denoted hereforth MBaL-30, MBaL-60, and MBaL-80 were isolated from seeds extract of Momordica balsamina by 30%, 60%, and 80% ammonium sulfate saturations, respectively. The native molecular weights of these lectins, as judged by gel filtration, were 108, 56, and 160 kDa,
Immunoadjuvant activity of crude lectin extracted from Momordica charantia seed.
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The aim of this study is to investigate the immunoadjuvant activity of the crude Momordica charantia lectin (crMCL) extracted from seed using beta-galactosidase (beta-gal) as the model antigen. BALB/c mice were injected intramuscularly with beta-gal alone or beta-gal + crMCL for up to four
Fluorescence quenching and time-resolved fluorescence studies on Momordica charantia (bitter gourd) seed lectin.
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Chemical modification studies implicated tryptophan (Trp) residues in the sugar binding activity of Momordica charantia lectin (MCL) [Mazumdar, T., Gaur, N. & Surolia, A. (1981) Eur. J. Biochem. 113, 463-470]. In the present study, the accessibility and environment of Trp residues in MCL were
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