The human invariant chain is the core protein of the human class II- associated proteoglycan
| Autor: | Andrea J. Sant, J Gorka, Vito Quaranta, Chris Bono, D M O'Sullivan, K S Giacoletto, Benjamin D. Schwartz |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1986 |
| Předmět: |
animal structures
Immunoprecipitation medicine.drug_class Immunology Cell Peptide Biology Monoclonal antibody chemistry.chemical_compound Methionine Antigen medicine Immunology and Allergy Humans chemistry.chemical_classification Histocompatibility Antigens Class II Articles Molecular biology Chondroitinases and Chondroitin Lyases Antigens Differentiation B-Lymphocyte Molecular Weight medicine.anatomical_structure chemistry Biochemistry Proteoglycan Chondroitin Sulfate Proteoglycans Solubility Chondroitin sulfate proteoglycan Chromobox Protein Homolog 5 embryonic structures biology.protein Electrophoresis Polyacrylamide Gel Proteoglycans |
| Zdroj: | The Journal of Experimental Medicine |
| ISSN: | 1540-9538 0022-1007 |
| Popis: | The human class II-associated chondroitin sulfate proteoglycan (CSPG) was analyzed biochemically and immunologically to determine a possible relationship with the human invariant chain (gamma 1) and its related components. The CSPG was purified by a three-step procedure involving associative ion-exchange chromatography, immunoprecipitation, and dissociative ion-exchange chromatography. Treatment of the CSPG with chondroitinase revealed core proteins of Mr approximately 46,000, 38,000, and 28,000, with the 38,000 species most highly represented. Tryptic peptide analysis revealed identity of the peptides of the 38,000 Mr core protein and gamma 1, and of the 28,000 Mr species and p25. The CSPG and its core proteins were shown to react directly with the mouse anti-human invariant chain monoclonal antibody VIC-Y1 and a rabbit antiserum produced against a synthetic peptide corresponding to the C-terminal end of invariant chain. These results demonstrate that the invariant chain is the core protein of the class II-associated CSPG. In addition, virtually all the CSPG was shown to be present on the cell surface. |
| Databáze: | OpenAIRE |
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