Mixed Micellization and Mixed Monolayer Formation of Sodium Cholate and Sodium Deoxycholate in Presence of Hydrophobic Salts Under Physiological Conditions

2013 ◽  
Vol 16 (6) ◽  
pp. 967-973 ◽  
Author(s):  
Muzaffar Hussain Najar ◽  
Oyais Ahmad Chat ◽  
Aijaz Ahmad Dar ◽  
Ghulam Mohammad Rather
1992 ◽  
Vol 149 (1) ◽  
pp. 216-225 ◽  
Author(s):  
Hidenori Miyoshi ◽  
Shigemi Nagadome ◽  
Gohsuke Sugihara ◽  
Hisao Kagimoto ◽  
Yoshitomi Ikawa ◽  
...  

RSC Advances ◽  
2015 ◽  
Vol 5 (88) ◽  
pp. 72132-72141 ◽  
Author(s):  
Rajni Vashishat ◽  
Reshu Sanan ◽  
Rakesh Kumar Mahajan

Solubilization of phenothiazine is studied. Phenothiazine is more solubilized in the core of mixed micelles of sodium deoxycholate and ionic liquid. Sodium deoxycholate is more hydrophobic in nature than sodium cholate.


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

Sign in / Sign up

Export Citation Format

Share Document