Improved secretion of human Fas ligand extracellular domain by N-terminal part truncation in Pichia pastoris and preparation of the N-linked carbohydrate chain trimmed derivative

Protein Expression and Purification

Volumn 60, Issue 2, 2008, Pages 205-213

  Muraki, Michiro ^a  

^a NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

Enzymatic deglycosylation; Extracellular domain; Human Fas ligand; N linked carbohydrate chain; Pichia pastoris; Preparation; Secretion level; Truncation

Indexed keywords

CARBOHYDRATE; FAS LIGAND; RECOMBINANT PROTEIN;

ARTICLE; CHEMISTRY; GENETICS; GLYCOSYLATION; HUMAN; ION EXCHANGE CHROMATOGRAPHY; ISOLATION AND PURIFICATION; MASS SPECTROMETRY; METABOLISM; PICHIA; POLYACRYLAMIDE GEL ELECTROPHORESIS;

CARBOHYDRATES; CHROMATOGRAPHY, ION EXCHANGE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FAS LIGAND PROTEIN; GLYCOSYLATION; HUMANS; PICHIA; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

PICHIA PASTORIS;

EID: 45449106344     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2008.03.027     Document Type: Article

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