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Self Purification of Two Serine Endopeptidases
We have reported that a serine protease from Pronase, homologous with bovine chymotrypsin, is both active and stable in 6 M guanidinium chloride. The present investigation examined the possibility that this unique property might be used to permit the enzyme to engage in its own purification by cleav...
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| Main Authors: | , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
1972
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC426988/ https://ncbi.nlm.nih.gov/pubmed/4506775 |
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