Literature DB >> 10419828

Expression of human gelatinase B in Pichia pastoris.

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.

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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


  2 in total

1.  Asn and asn: critical residues for in vitro biological activity of reteplase.

Authors:  Naganath Mandi; Kalyana R Sundaram; Sunil K Tandra; Suman Bandyopadhyay; Sriram Padmanabhan
Journal:  Adv Hematol       Date:  2010-06-21

Review 2.  Recombinant protein expression in Pichia pastoris.

Authors:  J M Cregg; J L Cereghino; J Shi; D R Higgins
Journal:  Mol Biotechnol       Date:  2000-09       Impact factor: 2.860

  2 in total

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