Document Detail

Expression of human gelatinase B in Pichia pastoris.
MedLine Citation:
PMID:  10419828     Owner:  NLM     Status:  MEDLINE    
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.
N Roy; S Padmanabhan; M Smith; L Shi; M Navre; G Das
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Protein expression and purification     Volume:  16     ISSN:  1046-5928     ISO Abbreviation:  Protein Expr. Purif.     Publication Date:  1999 Jul 
Date Detail:
Created Date:  1999-08-18     Completed Date:  1999-08-18     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9101496     Medline TA:  Protein Expr Purif     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  324-30     Citation Subset:  IM    
Copyright Information:
Copyright 1999 Academic Press.
Syngene Intl. Pvt. Ltd., Bangalore, 561229, India.
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MeSH Terms
Base Sequence
Chromatography, Affinity
Chromatography, Gel
Cloning, Molecular
Collagenases / genetics*,  isolation & purification
DNA Primers
Electrophoresis, Polyacrylamide Gel
Matrix Metalloproteinase 9
Pichia / genetics*
Recombinant Proteins / genetics,  isolation & purification
Reg. No./Substance:
0/DNA Primers; 0/Recombinant Proteins; EC 3.4.24.-/Collagenases; EC Metalloproteinase 9

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