Literature DB >> 762504

Immuno-chemical studies on the alkali-labile carbohydrate chains of human serum glycoproteins.

G Uhlenbruck, I Reese, P Vaith, H Haupt.   

Abstract

Human serum glycoproteins can be classified into those containing N-acetyl-D-galactosamine and into those lacking this hexosamine. The N-acetyl-D-galactosamine-containing serum glycoproteins have alkali-labile chains containing this hexosamine linked O-glycosidically to hydroxy amino acids. These alkali-labile chains can be demonstrated in neuraminic acid free serum glycoproteins by gas liquid chromatography and by using precipitating lectins from invertebrates and plants. They are represented by two chains, one containing only N-acetyl-D-galactosamine, the other with D-galactose linked (1--3) beta-glycosidically to this hexosamine forming a disaccharide. Serologically these two chains, which usually occur together on one molecule, can be characterized by their reaction with lectins from Helix pomatia (anti-A like) and from Agaricus bisporus and Arachis hypogaea (anti-TF specificity).

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Year:  1979        PMID: 762504     DOI: 10.1515/cclm.1979.17.1.29

Source DB:  PubMed          Journal:  J Clin Chem Clin Biochem        ISSN: 0340-076X


  2 in total

1.  The primary structure of human hemopexin deduced from cDNA sequence: evidence for internal, repeating homology.

Authors:  F Altruda; V Poli; G Restagno; P Argos; R Cortese; L Silengo
Journal:  Nucleic Acids Res       Date:  1985-06-11       Impact factor: 16.971

2.  Structure of human hemopexin: O-glycosyl and N-glycosyl sites and unusual clustering of tryptophan residues.

Authors:  N Takahashi; Y Takahashi; F W Putnam
Journal:  Proc Natl Acad Sci U S A       Date:  1984-04       Impact factor: 11.205

  2 in total

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