Repetitive Sequences in Protein A from Staphylococcus aureus. Arrangement of Five Regions within the Protein, Four being Highly Homologous and Fc-Binding
| Autor: | Jörgen Sjödahl |
|---|---|
| Rok vydání: | 1977 |
| Předmět: |
Staphylococcus aureus
Erythrocytes Protein Conformation Plasma protein binding Biology medicine.disease_cause Biochemistry Protein structure Bacterial Proteins medicine Animals Trypsin Amino Acid Sequence Amino Acids Binding site Peptide sequence Sheep Lysostaphin Circular Dichroism Immunoglobulin Fc Fragments Hemagglutination Tests Hemagglutination Inhibition Tests Peptide Fragments biology.protein Spectrophotometry Ultraviolet Binding Sites Antibody Protein A Protein Binding |
| Zdroj: | European Journal of Biochemistry. 73:343-351 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1977.tb11324.x |
| Popis: | After tryptic digestion of intact Staphylococcus aureus the residual portion of protein A that was still bound to the cell wall was cleaved off with lysostaphin. From the two digests Fc-binding fragments were isolated and the following characteristics observed. (a) There are four Fc-binding, highly homologous regions, each consisting of 58--62 amino acid residues. (b) These regions are consecutively arranged from the N-terminal part of the protein. (c) The residual C-terminal part, approximately 150-residues long, differs to a great extent with respect to primary and secondary structures from the four active regions. Furthermore, it is suggested that the protein is bound to the bacterial cell wall structure through this C-terminal part. |
| Databáze: | OpenAIRE |
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