TAILIEUCHUNG - Anthranilate synthetase from Escherichia coli SJHI: Purification and some properties

A procedure employed in the purification of anthranilate synhetase of Escherichia coli SJHI is described. The purified anthranilate synthetase appeared to be homogeneous when examined with poliacrylamide gel electrophoresis. Phenly-sepharose CL-4B and Blue dye sepharose were used for purification. | Tr. J. of Biology 23 (1999) 169-175 © TÜBİTAK Anthranilate Synthetase From Escherichia coli SJHI: Purification and Some Properties Münevver ARISOY Ankara University, Faculty of Health Education, Keçiören, Ankara-TURKEY Received: Abstract: A procedure employed in the purification of anthranilate synhetase of Escherichia coli SJHI is described. The purified anthranilate synthetase appeared to be homogeneous when examined with poliacrylamide gel electrophoresis. Phenly-sepharose CL-4B and Blue dye sepharose were used for purification. A positive correlation was found between purification and ammonium sulfate especially using concentrations greater than 10%. A positive effect 2-Mercapto-ethanol on the enzyme stability was also determined. Key Words: Purification, Anthranilate synthetase, Escherichia coli SJHI. Antranilat Sentatazın Escherichia coli SJHI’dan Saflaştırılması ve Özellikleri Özet: Bu çalışmada Escherichia coli SJHI dan antranilat sentatazın saflaştırılmasına ilişkin bir yöntem verilmiştir. Saflaştırılmış antranilat sentataz poliakrilamid jel elektroforezinde gözlenmiştir. Saflaştırma için Phenyl-sepharose CL-4B ve Blue dye sepharose kullanılmıştır. Amonyum sülfatın özellikle 10% dan büyük konsantrasyonları kullanıldığında saflaştırma ile aralarında pozitif bir ilişki olduğu saptanmıştır. Ayrıca enzimin stabilitesi üzerine 2-Mercapto-ethanol ün de olumlu bir etkisi olduğu gözlenmiştir. Anahtar Sözcükler: Saflaştırma, antranilat sentataz, Escherichia coli SJHI. Introduction Trytophan notable for its variety of important metabolic reactions and products was among the first amino acids shown to be nutritionally essential (1). The activity of anthranilate synthetase, the first enzyme in the L-tryptophan terminal pathway (2, 3, 4), has been regulated by L-trytophan in some bacteria (Escherichia coli SJHI, Aerobacter aerogenes, Bacillus subtilis, Pseudomonas putida, Brevibacterium flavum), yeast (Sacchoromyces cerevisia) and a fungus (Neurospora .

• Sinh học
• Anthranilate synthetase
• Escherichia coli SJHI
• Anthranilate synthetase
• Poliacrylamide gel electrophoresis
• Phenly sepharose CL 4B
• Blue dye sepharose