| Literature DB >> 10419828 |
N Roy1, S Padmanabhan, M Smith, L Shi, M Navre, G Das.
Abstract
Full-length human gelatinase B (FLGelB) and its C-terminal truncated form (dGelB) were expressed in Pichia pastoris strain GS115, using the Saccharomyces cerevisiae Mat alpha signal peptide. In both cases, a high level of the secreted protein could be detected by SDS-PAGE. The truncated gene was also expressed using the human gelatinase B native signal peptide. Secretion using the Mat alpha signal peptide was significantly greater than that from the native signal peptide. The recombinant products were purified and characterized biochemically. The recombinant proteins, FLGelB and dGelB, were found to have similar biochemical properties and activity to that of the human gelatinase B native protein. Copyright 1999 Academic Press.Entities:
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Year: 1999 PMID: 10419828 DOI: 10.1006/prep.1999.1073
Source DB: PubMed Journal: Protein Expr Purif ISSN: 1046-5928 Impact factor: 1.650