Asn to Lys mutations at three sites which are N-glycosylated in the mammalian protein decrease the aggregation of Escherichia coli-derived erythropoietin

Protein Engineering

Volumn 14, Issue 2, 2001, Pages 135-140

  Narhi, Linda O ^a   Arakawa, Tsutomu ^b   Aoki, Kenneth ^a   Wen, Jie ^a   Elliot, Steve ^a   Boone, Thomas ^a   Cheetham, Janet ^a  

^a AMGEN INC   (United States)

^b ALLIANCE PROTEIN LABORATORIES   (United States)

Author keywords

NMR; Protein conformation; Protein engineering; Protein stability

Indexed keywords

AMINO ACID; ASPARAGINE; CELL SURFACE RECEPTOR; CORE PROTEIN; ERYTHROPOIETIN; LYSINE; MUTANT PROTEIN; UREA;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; DIMERIZATION; ELECTRICITY; ESCHERICHIA COLI; HEAT TREATMENT; HIGH TEMPERATURE; ISOELECTRIC POINT; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN GLYCOSYLATION; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; RECEPTOR BINDING; STRUCTURE ANALYSIS; TEMPERATURE;

EID: 0035042650     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/14.2.135     Document Type: Article

References (24)