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Musa paradisiac : Banana
BanLec-I
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Molecular structure of
Banana:BanLec-I
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Musa paradisiac
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| Lecster ID:454 | Edit Entry |
| Source Organism: | Banana |
| Species: | Musa paradisiac |
| Common Nomenclature: | BanLec-I |
| Class: | ? |
| Index Nomenclature: | LECp.Mus.Par.fr.Hmg1 |
| Characterization Notes: | BanLec-I was found to be very effective as a probe in detecting glycoproteins, e.g. on nitrocellulose blots. For BanLec-I effect on IgG4, see: Int Arch Allergy Immunol. 1992;97(1):17-24. Banana lectin found in prepared food was found to be autoclave resistant, and indeed was enhanced by heating. See: Appl Environ Microbiol 1981 (41) 880-888 |
| Biological Activity: | The lectin does not agglutinate untreated human or sheep erythrocytes but does agglutinate rabbit red blood cells. Banana lectin also stimulates T-cell proliferation. See: Biochem J 1990 (272);721-726 IgG4 antibodies to banana were found to occur more frequently than expected. The most imprtant antigen involved is the lectin BanLec-I. See: Inter Archiv Allergy Immunol 1992 (97); 17-24 |
| Source Tissue: | Fruit |
| Specificity: | Man (alpha-methyl mannoside >Man/Glc) BanLec-I has a binding specificity for oligomannosidic glycans of size classes higher than (Man)6GlcNAc |
| Inhibitors: | |
| References: | Biochem J 1990 Dec 15;272(3):721-6 |
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