L-asparaginase of Thermus thermophilus: Purification, properties and identification of essential amino acids for its catalytic activity

Molecular and Cellular Biochemistry

Volumn 216, Issue 1-2, 2001, Pages 93-101

  Pritsa, A A ^a   Kyriakidis, D A ^a  

^a ARISTOTLE UNIVERSITY OF THESSALONIKI   (Greece)

Author keywords

Active site; L asparaginase; Purification; Renaturation; Thermostable; Thermus thermophilus

Indexed keywords

ARGININE; ASPARAGINASE; CARBOXYLIC ACID; CYSTEINE; ESSENTIAL AMINO ACID; HISTIDINE; SERINE;

ARTICLE; CATALYSIS; CHEMICAL MODIFICATION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ISOLATION; ENZYME PURIFICATION; MOLECULAR WEIGHT; NONHUMAN; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; THERMOPHILIC BACTERIUM; THERMOSTABILITY; THERMUS THERMOPHILUS;

ALKALINE PHOSPHATASE; AMINO ACIDS; ARGININE; ASPARAGINASE; BINDING SITES; CATALYSIS; CHROMATOGRAPHY, AGAROSE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HISTIDINE; HYDROGEN-ION CONCENTRATION; ISOELECTRIC FOCUSING; KINETICS; PROTEIN DENATURATION; TEMPERATURE; THERMUS THERMOPHILUS; TIME FACTORS;

BACTERIA (MICROORGANISMS); THERMUS THERMOPHILUS;

EID: 0035125429     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1011066129771     Document Type: Article

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