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- W2016243586 abstract "Incubation of human vitamin D3-binding protein (Gc protein), with a mixture of immobilized β-galactosidase and sialidase, efficiently generated a potent macrophage activating factor, a protein with N-acetylgalactosamine as the remaining sugar. Stepwise incubation of Gc protein with immobilized β-galactosidase and sialidase, and isolation of the intermediates with immobilized lectins, revealed that either sequence of hydrolysis of Gc glycoprotein by these glycosidases yields the macrophage-activating factor, implying that Gc protein carries a trisaccharide composed of N-acetylgalactosamine and dibranched galactose and sialic acid termini. A 3 hr incubation of mouse peritoneal macrophages with picomolar amounts of the enzymatically generated macrophage-activating factor (GcMAF) resulted in a greatly enhanced phagocytic activity. Administration of a minute amount (10–50 pg/mouse) of GcMAF resulted in a seven- to nine-fold enhanced phagocytic activity of macrophages. Injection of sheep red blood cells (SRBC) along with GcMAF into mice produced a large number of anti-SRBC antibody secreting splenic cells in 2–4 days." @default.
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- W2016243586 date "1996-10-01" @default.
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- W2016243586 title "Structural definition of a potent macrophage activating factor derived from vitamin D3-binding protein with adjuvant activity for antibody production" @default.
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- W2016243586 doi "https://doi.org/10.1016/s0161-5890(96)00081-8" @default.
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