Literature DB >> 701260

The asparagine-linked sugar chains of subcomponent C1q of the first component of human complement.

T Mizuochi, K Yonemasu, K Yamashita, A Kobata.   

Abstract

Human C1q, a subcomponent of the first component of complement, contains six asparagine-linked sugar chains in 1 molecule. The sugar chains are exclusively located in the COOH-terminal globular region which is composed of 330 amino acid residues. The sugar chains were liberated from the polypeptide portion by hydrazinolysis, and their structures were studied by the combination of sequential exoglycosidase digestion and methylation analysis. Based on the results, the structures NeuAcalpha2 leads to 6Galbeta1 leads to 4GlcNAcbeta1 leads to 2Manalpha1 leads to 6(+/- NeuAcalpha2 leads to 6Galbeta1 leads to 4GlcNAcbeta1 leads to 2Manalpha1 leads to 3)Manbeta1 leads to 4GlcNAcbeta1 leads to 4(+/-Fucalpha1 leads to 6)GlcNAc were confirmed.

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Year:  1978        PMID: 701260

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  19 in total

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3.  Semliki Forest virus glycans analyzed by affinity chromatography, hydrazinolysis and paper chromatography.

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4.  Fast sequencing of oligosaccharides: the reagent-array analysis method.

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6.  Analysis of human C1q by combined bottom-up and top-down mass spectrometry: detailed mapping of post-translational modifications and insights into the C1r/C1s binding sites.

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7.  Evidence for the presence and structure of asparagine-linked oligosaccharide units in the core protein of proteodermatan sulphate.

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8.  Glycoprotein biosynthesis in quiescent and stimulated thymocytes and a T-cell lymphoma.

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9.  Hydroxylysine-linked glycosides of human complement subcomponent C1q and various collagens.

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10.  Carbohydrate-structure-dependent recognition of desialylated serum glycoproteins in the liver and leucocytes. Two complementary systems.

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