Unfolding of human secretory immunoglobulin A
| Autor: | Per Brandtzaeg |
|---|---|
| Rok vydání: | 1970 |
| Předmět: |
Immunoglobulin A
Immunodiffusion Protein subunit Immunology Physical Therapy Sports Therapy and Rehabilitation Secretory Immunoglobulin A Sulfides Humans Non-covalent interactions Secretory Piece Molecular Biology chemistry.chemical_classification biology Colostrum Rehabilitation Disulfide bond General Medicine Models Structural chemistry Biochemistry Immunoglobulin G Biophysics biology.protein Protein quaternary structure gamma-Globulins Haptens |
| Zdroj: | Immunochemistry. 7:127-130 |
| ISSN: | 0019-2791 |
| DOI: | 10.1016/0019-2791(70)90037-6 |
| Popis: | The quaternary structure of human secretory immunoglobulin A is stabilized by noncovalent forces to a degree that certain antigenic determinants of the secretory piece subunit are inaccessible. The strength of these noncovalent interactions depends on the presence of disulfide bonds linking the secretory piece to the immunoglobulin A subunits. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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