scholarly journals Purification and Characterization of a New Anti-Nucleating Protein Isolated from Acinetobacter calcoaceticus KINI-1

1996 ◽  
Vol 1 (1) ◽  
pp. 11-17 ◽  
Author(s):  
HIDEHISA KAWAHARA ◽  
ISAO NAGAE ◽  
HITOSHI OBATA
Keyword(s):  
Acinetobacter Calcoaceticus ◽  
Purification And Characterization

Purification and characterization of rhodanese from Acinetobacter calcoaceticus

1980 ◽  
Vol 26 (3) ◽  
pp. 281-286 ◽  
Author(s):  
Peter A. Vandenbergh ◽  
Richard S. Berk
Keyword(s):  
Reduced Glutathione ◽  
Acinetobacter Calcoaceticus ◽  
Sucrose Density Gradient ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Soluble Enzyme ◽  
Purification And Characterization ◽  
Ph Optimum ◽  
Intracellular Enzyme

Rhodanese (thiosulfate: cyanide sulfur transferase, EC 2.8.1.1) was found to be constitutively present as an intracellular enzyme in Acinetobacter calcoaceticus. The soluble enzyme was purified 40.9-fold by a procedure which included ultracentrifugation, ethanol precipitation, CM-Sephadex batchwise separation, QAE-50 ion exchange chromatography, and sucrose density gradient ultracentrifugation. The enzyme had a molecular weight of approximately 35 000 with a pH optimum of 8–8.5. Activity was substantially enhanced by supplements of 2-mercaptoethanol and to a lesser extent by cysteine–HCl or reduced glutathione. No degradation of the enzyme into smaller subunits was observed when treated with 2-mercaptoethanol.

Sign in / Sign up

Export Citation Format

Share Document