On the interpretation of transport properties of sodium cholate and sodium deoxycholate in binary and ternary aqueous mixtures

2011 ◽  
Vol 13 (35) ◽  
pp. 15906 ◽  
Author(s):  
Gaetano Mangiapia ◽  
Gerardino D'Errico ◽  
Fabio Capuano ◽  
Ornella Ortona ◽  
Richard K. Heenan ◽  
...  
2006 ◽  
Vol 27 (8) ◽  
pp. 1099-1111 ◽  
Author(s):  
M. Vinceković ◽  
D. Jurašin ◽  
V. Tomašić ◽  
M. Bujan ◽  
N. Filipović‐Vinceković

1981 ◽  
Vol 36 (5-6) ◽  
pp. 400-406 ◽  
Author(s):  
Toshihisa Ohshima ◽  
Gerhart Drews

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.


2001 ◽  
Vol 120 (5) ◽  
pp. A203
Author(s):  
L. Zhang ◽  
Z.L. Yang ◽  
Roger D. Soloway ◽  
S.F. Weng ◽  
J.G. Wu

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