Improvement in performance of affinity gels containing Gly-D-Phe as a ligand to thermolysin due to increasing the spacer chain length

Bioscience, Biotechnology and Biochemistry

Volumn 71, Issue 8, 2007, Pages 2083-2086

  Inouye, Kuniyo ^a   Nakamura, Koji ^b   Kusano, Masayuki ^a   Yasukawa, Kiyoshi ^a  

^a KYOTO UNIVERSITY   (Japan)

^b TOSOH CORPORATION   (Japan)

Author keywords

Affinity chromatography; Glycyl D phenylalanine; Metalloproteinase; Spacer chain length; Thermolysin

Indexed keywords

ADSORPTION ISOTHERMS; AFFINITY CHROMATOGRAPHY; COLUMN CHROMATOGRAPHY; ENZYME IMMOBILIZATION; LIGANDS;

GLYCYL-D-PHENYLALANINE; METALLOPROTEINASE; SPACER CHAIN LENGTH; THERMOLYSIN;

GELS;

CROSS LINKING REAGENT; DIPEPTIDE; GLYCYLPHENYLALANINE; LIGAND; RESIN; THERMOLYSIN;

AFFINITY CHROMATOGRAPHY; ARTICLE; CHEMISTRY; GEL; ISOLATION AND PURIFICATION; METHODOLOGY; PROTEIN BINDING; STANDARD; TEMPERATURE;

CHROMATOGRAPHY, AFFINITY; CROSS-LINKING REAGENTS; DIPEPTIDES; GELS; LIGANDS; PROTEIN BINDING; RESINS, SYNTHETIC; TEMPERATURE; THERMOLYSIN;

EID: 36148935972     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70178     Document Type: Article

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