The present study investigates the chemical structure of a ganglioside, detected by monoclonal antibody (MAb) MacG1, which reacts with intracytoplasmic granules of tumor-infiltrating macrophages. The results obtained by enzymatic hydrolysis and fast-atom bombardment-mass spectrometry reveal that MAb MacG1 reacts with a subcomponent of the ganglioside GM3 found in melanoma and bovine brain. MAb MacG1 might be a powerful tool to distinguish among GM3 species and could help to define their possibly different biological functions.

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http://dx.doi.org/10.1089/hyb.1989.8.153DOI Listing

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The present study investigates the chemical structure of a ganglioside, detected by monoclonal antibody (MAb) MacG1, which reacts with intracytoplasmic granules of tumor-infiltrating macrophages. The results obtained by enzymatic hydrolysis and fast-atom bombardment-mass spectrometry reveal that MAb MacG1 reacts with a subcomponent of the ganglioside GM3 found in melanoma and bovine brain. MAb MacG1 might be a powerful tool to distinguish among GM3 species and could help to define their possibly different biological functions.

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Monoclonal antibody (mAb) MacG1 was recently shown to detect a monosialoganglioside expressed in tumor infiltrating macrophages. The present study demonstrates with in vitro experiments that the MacG1 epitope is generated during cellular digestion in phagocytic monocytes. Following phagocytosis and degradation of MacG1 negative sheep red blood cells, the MacG1 epitope was expressed in intracytoplamsic granules of murine plastic-adherent peritoneal cells.

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MacG1 is a mouse monoclonal antibody (mAb) directed against a ganglioside, which is differentially expressed by macrophages infiltrating malignant melanomas and benign melanocytic lesions. mAb MacG1 was obtained by immunization with liposomes containing a mixture of gangliosides extracted from malignant melanoma. The antibody was selected for binding to melanoma gangliosides and for reactivity with frozen tissue sections of malignant melanoma.

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