Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin)
Autor: | Johann Schaller, M A Hediger, Thomas M. Marti, H Haupt, Karl Schmid, Michael Walsh, Reinhard Brossmer, Gwynneth D. Offner, K Takagaki, J H Collins |
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Rok vydání: | 1992 |
Předmět: |
Proteases
Protein Conformation Sialoglycoproteins Molecular Sequence Data Peptide Biology Serine Antigens CD Humans Amino Acid Sequence Threonine Peptide sequence Glycoproteins chemistry.chemical_classification Alanine CD43 Leukosialin Multidisciplinary Glycopeptides Blood Proteins Molecular biology Peptide Fragments Molecular Weight N-terminus Carbohydrate Sequence chemistry Biochemistry Research Article |
Zdroj: | Proceedings of the National Academy of Sciences. 89:663-667 |
ISSN: | 1091-6490 0027-8424 |
Popis: | The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases. This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans. Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated. The homogeneous N terminus was established as serine. C-terminal analysis revealed multiple C-terminal residues, suggesting that galactoglycoprotein molecules are of varying lengths. A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin). Further support of the relatedness of these molecules was obtained by immunoprecipitation of 125I-labeled galactoglycoprotein by monoclonal anti-CD43 antibodies. The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets. |
Databáze: | OpenAIRE |
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