Solute–solvent interactions in micellar electrokinetic chromatography: VII. Characterization of sodium cholate–sodium deoxycholate mixed-micellar systems

2010 ◽  
Vol 1217 (10) ◽  
pp. 1701-1708 ◽  
Author(s):  
Marta Hidalgo-Rodríguez ◽  
Elisabet Fuguet ◽  
Clara Ràfols ◽  
Martí Rosés
Keyword(s):  
Micellar Electrokinetic Chromatography ◽  
Sodium Deoxycholate ◽  
Sodium Cholate ◽  
Electrokinetic Chromatography ◽  
Solvent Interactions ◽  
Micellar Systems

Characterization of chemical selectivity in micellar electrokinetic chromatography

2000 ◽  
Vol 888 (1-2) ◽  
pp. 229-240 ◽  
Author(s):  
Mark D. Trone ◽  
Juan P. Mack ◽  
Henry P. Goodell ◽  
Morteza G. Khaledi
Keyword(s):  
Micellar Electrokinetic Chromatography ◽  
Electrokinetic Chromatography ◽  
Chemical Selectivity

Isolation and Partial Characterization of the Membrane-Bound NADH Dehydrogenase from the Phototrophic Bacterium Rhodopseudomonas capsulata

1981 ◽  
Vol 36 (5-6) ◽  
pp. 400-406 ◽  
Author(s):  
Toshihisa Ohshima ◽  
Gerhart Drews
Keyword(s):  
Nadh Dehydrogenase ◽  
Deae Cellulose ◽  
Sodium Deoxycholate ◽  
Pyridine Nucleotide ◽  
Sodium Cholate ◽  
Rhodopseudomonas Capsulata ◽  
Michaelis Constant ◽  
Membrane Bound ◽  
Ph Dependent

Abstract Chemotrophically grown cells of Rhodopseudomonas capsulata contain at least three different pyridine nucleotide dehydrogenases, i) a soluble, found in the supernatant (144000 × g) of cell free extracts, NADH-dependent, ii) a mem brane-bound, NADH-dependent, and iii) a soluble, found in the supernatant N AD PH dependent. The membrane-bound NADH dehydrogenase (E.C. 1.6.99.3) has been solubilized by sodium deoxycholate treatm ent of m em branes and purified 75 fold by column chrom atography on Sephadex G-150 and DEAE cellulose in the presence of sodium cholate. The native enzyme has an apparent molecular mass (Mr) of 97 000, containing polypeptides of Mr of about 15 000. The pH optim um was at 7.5. The enzyme was specific for NADH. The Michaelis constant for NADH and DCIP were 4.0 and 63 μm, respectively. The enzyme was inactivated by FMN, riboflavin and NADH. In contrast, the soluble NADH-dehydrogenase (i) was activated by FMN.

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