A mutant trypsin-like enzyme from Streptomyces fradiae, created by site-directed mutagenesis, improves affinity chromatography for protein trypsin inhibitors

Applied Microbiology and Biotechnology

Volumn 46, Issue 1, 1996, Pages 15-21

  Katoh, T ^a   Kikuchi, N ^a   Nagata, K ^a   Yoshida, N ^a  

^a SHIONOGI AND CO LTD   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; TRYPSIN; TRYPSIN INHIBITOR;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; GENE MUTATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; NONHUMAN; SITE DIRECTED MUTAGENESIS; STREPTOMYCES;

CHROMATOGRAPHY, AFFINITY; HUMANS; KINETICS; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; RECOMBINANT PROTEINS; STREPTOMYCES; TRYPSIN; TRYPSIN INHIBITOR, KAZAL PANCREATIC; TRYPSIN INHIBITORS;

GLYCINE MAX; SACCHAROMYCES CEREVISIAE; STREPTOMYCES; STREPTOMYCES FRADIAE; STREPTOMYCES LIVIDANS;

EID: 0029793288     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002530050777     Document Type: Article

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