Recombinant human mast-cell chymase: An improved procedure for expression in Pichia pastoris and purification of the highly active enzyme

Biotechnology and Applied Biochemistry

Volumn 41, Issue 1, 2005, Pages 89-95

  Lockhart, Brent E ^a   Vencill, Jessica R ^a   Felix, Cherise M ^a   Johnson, David A ^a  

^a East Tennessee State University   (United States)

Author keywords

Chymase; Fermentation; Heparin; Human mast cell; Pichia pastoris; Secretion

Indexed keywords

AFFINITY CHROMATOGRAPHY; CELL CULTURE; DNA; ENZYMES; FERMENTATION; GENES;

CHYMASE; FERMENTORS; HEPARIN; PICHIA PASTORIS;

CELLS;

CHYMASE; CHYMOTRYPSIN; COMPLEMENTARY DNA; HEPARIN; METHANOL; RECOMBINANT CHYMASE; SERINE PROTEINASE; UNCLASSIFIED DRUG;

AFFINITY CHROMATOGRAPHY; ARTICLE; CELL GRANULE; CULTURE MEDIUM; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; FERMENTATION TECHNIQUE; HOMOLOGOUS RECOMBINATION; HUMAN; HUMAN CELL; HYDROPHOBICITY; IMMOBILIZATION; MAST CELL; NONHUMAN; PICHIA PASTORIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRODUCT RECOVERY; SCREENING TEST;

CELL CULTURE TECHNIQUES; CHYMASES; CLONING, MOLECULAR; ENZYME ACTIVATION; ENZYME STABILITY; GENE EXPRESSION REGULATION, FUNGAL; GENETIC ENHANCEMENT; HUMANS; MAST CELLS; MOLECULAR WEIGHT; PICHIA; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; SERINE ENDOPEPTIDASES;

PICHIA; PICHIA PASTORIS;

EID: 12544250265     PISSN: 08854513     EISSN: None     Source Type: Journal    
DOI: 10.1042/BA20040074     Document Type: Article

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