Amino acid sequence of bovine white matter proteolipid
| Autor: | Mohammed Samiullah, Betty H. Chao, Marjorie B. Lees, Richard A. Laursen, Leu-Fen H. Lin |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Proteolipid protein 1
Biophysics Biochemistry medicine Animals Chymotrypsin Trypsin Amino Acid Sequence Myelin Proteolipid Protein Molecular Biology Peptide sequence Myelin proteolipid Brain Chemistry Clostripain biology Protein primary structure Proteolytic enzymes Peptide Fragments Skatole Molecular Weight biology.protein Cattle Myelin Proteins medicine.drug |
| Zdroj: | Archives of Biochemistry and Biophysics. 226:643-656 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/0003-9861(83)90334-x |
| Popis: | The sequence of the bovine white matter proteolipid has been studied by a combination of proteolytic digestion and chemical cleavage at tryptophan residues. Alignment of peptides obtained by digestion with trypsin, chymotrypsin, clostripain, and Staphylococcus aureus protease gave the sequence of 52 residues at the amino terminus, 96 residues at the carboxyl terminus, and several additional segments. Peptides obtained by treatment of the protein with 2-(2-nitrophenylsulfenyl)-3-methyl-3′-bromoindolenine confirmed the alignment and extended the sequence. This information, combined with that of other investigators, permits us to propose the primary structure for the entire protein. On the basis of the sequence determination, the molecular weight of the proteolipid protein is 29,869. |
| Databáze: | OpenAIRE |
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