Enzymological properties of pantothenate synthetase from Escherichia coli B.

Enzymological properties of pantothenate synthetase from Escherichia coli B.

Following a previous report on physicochemical properties, the enzymological properties of a homogeneously purified preparation of pantothenate synthetase were described. The optimum pH was 10.0 and optimum temperature 30 degrees C. The lyophilized enzyme was very stable on standing at -20 degrees C. K+ or NH4+ and Mg2+ were required as activators; other cations examined were inhibitive to vari...

Partial purification and properties of phosphatidylserine synthetase from Escherichia coli.

CDP-diglyceride: L-serine phosphatidyltransferase (phosphatidylserine synthetase) of Escherichia coli is tightly associated with ribosomes in crude cell-free extracts. The synthetase has now been separated from ribosomes by extraction with solutions containing 5 M NaCl and has been purified loo-fold. The partially purified enzyme is devoid of contaminating hydrolytic activities and nearly free ...

Anthranilate Synthetase From Escherichia coli SJHI: Purification and Some Properties

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 us...

The isolation and properties of phenylalanyl ribonucleic acid synthetase from Escherichia coli B.

Phenylalanyl ribonucleic acid synthetase has been isolated frcm Escherichia coli and is 93% pure as determined by analytical centrifugation and gel electrophoresis. The procedure is adaptable to large scale preparation. No other aminoacyl-RNA synthetases are present in the purified preparation. The molecular weight of the enzyme is 181,000, with an ~~0,~ of 8.6. Optimal reaction conditions have...

Isoleucyl-tRNA synthetase. A fluorescence study of the binding properties of the synthetase from Escherichia coli.