Characterization of the oligosaccharide units of the fourth component of complement (Ss protein) synthesized by murine macrophages

M. H. Roos; S. Kornfeld; D. C. Shreffler

Characterization of the oligosaccharide units of the fourth component of complement (Ss protein) synthesized by murine macrophages

M. H. Roos, S. Kornfeld, D. C. Shreffler

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Abstract

The glycosylation of murine C4 (Ss protein) synthesized by peritoneal macrophages has been investigated. Both the intracellular precursor, P-C4 (185), and the C4 α- and β-chains that were secreted into medium were found to be glycosylated; however, no carbohydrate units were detected on the γ-chain. Analyses of the oligosaccharide units showed that P-C4 (185) appears to contain both a 'complex' and a 'high mannose' carbohydrate group, the α-chain a 'complex' group and the β-chain a 'high mannose' carbohydrate unit.

Original language	English
Pages (from-to)	2860-2863
Number of pages	4
Journal	Journal of Immunology
Volume	124
Issue number	6
State	Published - Jan 1 1980

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abstract = "The glycosylation of murine C4 (Ss protein) synthesized by peritoneal macrophages has been investigated. Both the intracellular precursor, P-C4 (185), and the C4 α- and β-chains that were secreted into medium were found to be glycosylated; however, no carbohydrate units were detected on the γ-chain. Analyses of the oligosaccharide units showed that P-C4 (185) appears to contain both a 'complex' and a 'high mannose' carbohydrate group, the α-chain a 'complex' group and the β-chain a 'high mannose' carbohydrate unit.",

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AU - Kornfeld, S.

AU - Shreffler, D. C.

PY - 1980/1/1

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N2 - The glycosylation of murine C4 (Ss protein) synthesized by peritoneal macrophages has been investigated. Both the intracellular precursor, P-C4 (185), and the C4 α- and β-chains that were secreted into medium were found to be glycosylated; however, no carbohydrate units were detected on the γ-chain. Analyses of the oligosaccharide units showed that P-C4 (185) appears to contain both a 'complex' and a 'high mannose' carbohydrate group, the α-chain a 'complex' group and the β-chain a 'high mannose' carbohydrate unit.

AB - The glycosylation of murine C4 (Ss protein) synthesized by peritoneal macrophages has been investigated. Both the intracellular precursor, P-C4 (185), and the C4 α- and β-chains that were secreted into medium were found to be glycosylated; however, no carbohydrate units were detected on the γ-chain. Analyses of the oligosaccharide units showed that P-C4 (185) appears to contain both a 'complex' and a 'high mannose' carbohydrate group, the α-chain a 'complex' group and the β-chain a 'high mannose' carbohydrate unit.

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JO - Journal of Immunology

JF - Journal of Immunology

IS - 6

ER -

Characterization of the oligosaccharide units of the fourth component of complement (Ss protein) synthesized by murine macrophages

Abstract

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