A monoclonal antibody against erythrocyte spectrin reacts with both α- and β-subunits and detects spectrin-like molecules in non-erythroid cells
| Autor: | Janis Fleming, Paul Harrison, Kuppuswamy Kasturi |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Erythrocytes
medicine.drug_class T-Lymphocytes Monoclonal antibody Cell Line Epitopes Mice medicine Animals Spectrin Denaturation (biochemistry) Amino Acid Sequence Cytoskeleton biology Antibodies Monoclonal Membrane Proteins Cell Biology Fibroblasts Hematopoietic Stem Cells Molecular biology Blot Red blood cell medicine.anatomical_structure Biochemistry Cell culture biology.protein Antibody |
| Zdroj: | Experimental Cell Research. 144:241-247 |
| ISSN: | 0014-4827 |
| DOI: | 10.1016/0014-4827(83)90462-7 |
| Popis: | A panel of nine monoclonal antibodies against the characteristic erythrocyte membrane protein spectrin has been isolated. One antibody reacts with both the 240 000 and 220 000 D alpha- and beta-subunits of spectrin after denaturation. The same antibody reacts with a 240 000 D protein present in various hemopoietic and other cell lines, as well as some smaller polypeptides, as established by western blotting and immunoautoradiography. These results indicate that the alpha- and beta-subunits of spectrin, a polypeptide of 240 000, and some smaller polypeptides present in non-erythroid cell types possess a considerable region of sequence homology, but it is not yet clear just how extensively the spectrin-like molecules and other polypeptides are related. |
| Databáze: | OpenAIRE |
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