Comparison of two expression platforms in respect to protein yield and quality: Pichia pastoris versus Pichia angusta

Protein Expression and Purification

Volumn 66, Issue 2, 2009, Pages 165-171

  Mack, Matthias ^a   Wannemacher, Marion ^b   Hobl, Birgit ^a   Pietschmann, Patricia ^b   Hock, Björn ^b  

^a MANNHEIM UNIVERSITY OF APPLIED SCIENCES   (Germany)

^b Merck Serono GmbH   (Germany)

Author keywords

Expression systems; Pichia angusta; Pichia pastoris; Recombinant protein production

Indexed keywords

HGF PROTEIN, HUMAN; RECOMBINANT PROTEIN; SCATTER FACTOR; THROMBOPLASTIN;

AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; ARTICLE; BIOSYNTHESIS; COMPARATIVE STUDY; GENE DOSAGE; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; PICHIA; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN ENGINEERING; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, AFFINITY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GENE DOSAGE; HEPATOCYTE GROWTH FACTOR; MOLECULAR SEQUENCE DATA; PICHIA; PROTEIN ENGINEERING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; THROMBOPLASTIN;

MAMMALIA; PICHIA; PICHIA ANGUSTA; PICHIA PASTORIS; SACCHAROMYCES CEREVISIAE;

EID: 67349273072     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2009.03.010     Document Type: Article

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