N-terminal domain of pepsin as a model for retroviral dimeric aspartyl protease
| Autor: | Coletti-Previero Ma, M. Bianchi, Bertrand Castro, R.-A. Boigegrain |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Autolysis (biology)
Proteases Swine Stereochemistry Molecular Sequence Data Biophysics Biochemistry Chromatography Affinity Substrate Specificity Pepsin Affinity chromatography Endopeptidases Retroviral aspartyl protease Animals Aspartic Acid Endopeptidases Amino Acid Sequence Molecular Biology Peptide sequence chemistry.chemical_classification biology Chemistry Active site Cell Biology Pepsin A Amino acid Retroviridae biology.protein |
| Zdroj: | Biochemical and Biophysical Research Communications. 167:339-344 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(90)91770-s |
| Popis: | Autolysis of porcine pepsin at pH 4 affords a derivative possessing intrinsic proteolytic activity. This derivative was isolated by alumina pseudo-affinity chromatography and gel-filtration and was found to result from the tight association of two identical molecules, 135 amino acids long, emerging from the N-terminal domain of pepsin. This finding emphasizes a similarity with the only aspartyl-proteases known to act as dimers, the retroviral proteases. |
| Databáze: | OpenAIRE |
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