| Autor: |
R.-A. Boigegrain, L. Chiche, Coletti-Previero Ma, Hélène Mattras, M. Bianchi, B. Castro |
| Rok vydání: |
1991 |
| Předmět: |
|
| Zdroj: |
Methods in Protein Sequence Analysis ISBN: 9783034856805 |
| DOI: |
10.1007/978-3-0348-5678-2_24 |
| Popis: |
Autolysis of porcine pepsin yielded a fragment, showing proteolytic activity upon dimerization. This derivative was isolated by alumina with a new apparatus, conceived for affinity chromatography of dilute solutions. The similarities and the differences between the dimer and the parent pepsin are presented as well as the modelisation of the putative dimer and the behaviour of the molecule under dissociating and reassociating conditions. The dimer is an aspartic protease with new and sometimes unexpected characteristics, such as resistance to pH denaturation and autodigestion as well as a fair activity at subzero temperatures. The modelisation suggested that the dimerization process is compatible with the solvatation free energy, taken as a criterion to evaluate protein models. The model was compared with HIV protease, the only dimeric aspartic protease characterized at present. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
