Amino acid composition and proteolytic generated domains of higher plant tubulin
| Autor: | Iradj Amiri, Anne-Marie Lambert, Pascal Picquot, Marylin Vantard, Luc Fausser |
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| Rok vydání: | 1988 |
| Předmět: |
Macromolecular Substances
Swine Proteolysis Lysine Immunoblotting Biophysics macromolecular substances Biology Cleavage (embryo) Biochemistry Species Specificity Tubulin Sequence Homology Nucleic Acid medicine Animals Chymotrypsin Trypsin Amino Acid Sequence Amino Acids Molecular Biology Peptide sequence chemistry.chemical_classification medicine.diagnostic_test food and beverages Cell Biology Plants Molecular biology Peptide Fragments Amino acid chemistry biology.protein medicine.drug |
| Zdroj: | Biochemical and biophysical research communications. 156(1) |
| ISSN: | 0006-291X |
| Popis: | The molecular architecture of tubulin from higher plant remains unknown. In this report we have made an attempt to identify higher plant tubulin domains using total and limited proteolysis of Haemanthus endosperm tubulin. The tubulin was previously purified and characterized (Picquot and Lambert 1988). The amino acid composition revealed a high content of basic residues, such as arginine and lysine. Tubulin domains were probed by tryptic and chymotryptic cleavage and analyzed by immunoblotting using specific monoclonal antibodies against alpha or beta subunits. These data shed light on specific properties of the higher plant tubulin. |
| Databáze: | OpenAIRE |
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