Experimental allergic encephalomyelitis. Isolation of basic proteins and polypeptides from central nervous tissue
| Autor: | P. R. Carnegie, Beverley Bencina, G. Lamoureux |
|---|---|
| Rok vydání: | 1967 |
| Předmět: |
Electrophoresis
Male History Encephalomyelitis Autoimmune Experimental Chromatography Paper Proteolysis Encephalomyelitis Guinea Pigs Nerve Tissue Proteins Defatting Education Myelin medicine Animals Amino Acids chemistry.chemical_classification Brain Chemistry medicine.diagnostic_test Chemistry Nervous tissue Biological activity Articles medicine.disease Computer Science Applications Amino acid Molecular Weight medicine.anatomical_structure Biochemistry Spinal Cord Sephadex Chromatography Gel Cattle Peptides |
| Zdroj: | The Biochemical journal. 105(2) |
| ISSN: | 0264-6021 |
| Popis: | 1. Basic protein (mol.wt. 16500) and polypeptides (mol.wt. 3500) were isolated from bovine spinal cord by a procedure involving defatting, acid extraction of the defatted material and repeated chromatography on Sephadex G-50. Similar fractions were isolated from guinea-pig brain. 2. These fractions produced experimental allergic encephalomyelitis in guinea pigs. 3. The polypeptides appeared to be derived from a basic protein of myelin as a result of the action of an acid proteinase during extraction with acid. Similar proteolysis might also occur in the isolation of other biologically active polypeptides from acetone-dried powders of nervous tissue. The activity of the acid proteinase was lowered by defatting with chloroform–methanol. 4. Peptides from tryptic digests of encephalitogenic polypeptides and protein were also encephalitogenic, which suggests that the encephalitogenic determinant may be quite a short sequence of amino acids. 5. These encephalitogenic polypeptides are further examples of antigens of low molecular weight. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|