Crystallization of the fungal enzyme proteinase K and amino acid composition
| Autor: | J.K. Dattagupta, N.J. Pieniazek, T. Fujiwara, Philip C. Manor, E.V. Grishin, K. Lindner, Wolfram Saenger, D. Suck |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
chemistry.chemical_classification
biology Protein Conformation Proteinase K Amino acid law.invention Molecular Weight Serine Crystallography Enzyme Protein structure X-Ray Diffraction chemistry Amino acid composition Structural Biology law X-ray crystallography biology.protein Mitosporic Fungi Amino Acids Crystallization Molecular Biology Peptide Hydrolases |
| Zdroj: | Journal of Molecular Biology. 97:267-271 |
| ISSN: | 0022-2836 |
| Popis: | Proteinase K is obtained from the fungus Tritirachium album Limber and is named after its keratin-digesting activity. The enzyme, of molecular weight 18,500, is a serine proteinase and hydrolyses proteins at the carboxyl end of hydrophobic amino acids, as does α-chymotrypsin. The amino acid composition of proteinase K was determined by standard methods and the protein was crystallized using an improved dialysis method. The crystals obtained have been characterized by X-ray diffraction methods; the space group is tetragonal, P41212 or P43212 and the cell constants are a = b = 68·3 A, c = 108·5 A; two protein molecules are found in one asymmetric unit. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|