Effects of stepwise addition of HCl to sodium cholate and sodium deoxycholate micellar solutions

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

Effects of stepwise addition of HCl to sodium cholate and sodium deoxycholate micellar solutions

2001 ◽  
Vol 120 (5) ◽  
pp. A203-A203
Author(s):  
L ZHANG ◽  
Z YANG ◽  
R SOLOWAY ◽  
S WENG ◽  
J WU
Keyword(s):  
Sodium Deoxycholate ◽  
Sodium Cholate ◽  
Micellar Solutions

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.

scholarly journals Physical Characterization and Biodistribution of Cisplatin Loaded in Surfactant Modified-Hybrid Nanoparticles Using Polyethylene Oxide-b-Polymethacrylic Acid

2020 ◽  
Author(s):  
Andang Miatmoko
Keyword(s):  
Polyethylene Oxide ◽  
Tween 80 ◽  
Sodium Deoxycholate ◽  
Sodium Cholate ◽  
Hybrid Nanoparticles ◽  
Molar Ratio ◽  
Particle Sizes ◽  
Polymethacrylic Acid ◽  
Tumor Accumulation

Purpose: Conjugating cisplatin into hybrid nanoparticles is intended to enhance tumor accumulation due to drug interaction with polymer and prevent premature drug release because of the presence of a lipid layer. Methods: Hybrid nanoparticles composed of polyethylene oxide-b-polymethacrylic acid, egg phosphatidylcholine, and surfactant, i.e. sodium cholate/sodium deoxycholate/Tween 80, were prepared by the injection method. Cisplatin was subsequently loaded by incubating the polymer-drug mixtures at the molar ratio of carboxylate ions of 2:1. Results: The results showed that the addition of surfactants produced particle sizes between 33 and 52 nm. The addition of cisplatin increased the ζ-potential to slightly positive charges with encapsulation efficiencies of 5-18%. An in vivo biodistribution study of mice identified a cisplatin plasma concentration of sodium cholate-modified hybrid nanoparticles ten times higher than cisplatin solution, thus producing high tumor accumulation. Conclusion: Conjugating cisplatin into sodium cholate-modified hybrid nanoparticles improves its accumulation in tumors.

Substitution of Lipids with Bile Salts in the Formation of Thrombin

1969 ◽  
Vol 22 (01) ◽  
pp. 013-027 ◽  
Author(s):  
Monika Barthels ◽  
W. H Seegers
Keyword(s):  
Calcium Ions ◽  
Bile Salts ◽  
Thrombin Generation ◽  
Sodium Deoxycholate ◽  
Sodium Cholate ◽  
Phosphatidyl Serine ◽  
Molar Ratio ◽  
Platelet Factor ◽  
Analytical Reagents ◽  
Autoprothrombin C

SummaryThe generation of thrombin was studied in an activating system consisting of purified thrombin zymogens, purified autoprothrombin C, purified Ac-globulin, lipid or bile salts, and calcium chloride. With the concentration of calcium ions and pH fixed, the effect of varying the other three procoagulants was studied. Bile salts were effective substitutes for lipids in a concentration where micelles form. The approximate effectiveness from highest to lowest was: conjugated sodium salt of taurocholic acid, sodium cholate, sodium deoxycholate. Sodium dehydrocholate was ineffective. Autoprothrombin C is the enzyme for thrombin formation. For accelerating its activity best results were obtained with the simultaneous presence of optimal concentrations of calcium ions, Ac-globulin and lipids or bile salts. Reducing any one of the three to zero concentration decreased the rate and yield of thrombin generation.The form in which the zymogen is used was found to be important. Prothrombin complex, DE AE-prothrombin and prethrombin were studied. Each substrate has its peculiar requirements for yielding thrombin. Prothrombin complex and DEAE-pro-thrombin activated far more rapidly and required 10 times less autoprothrombin C than prethrombin. The yield of thrombin from these substrates was also higher than from prethrombin. DE AE-prothrombin required the least amount of lipid. For the bile salts the required concentrations were nearly always the same from one substrate to another. To a certain extent Benadryl could also be substituted for lipids. In association with rapid thrombin generation from DE AE-prothrombin the Ac-globulin and autoprothrombin C Avere represented in approximately a 6:1 molar ratio. As compared with the weight of the enzyme large amounts of Ac-globulin and cholate were required.DE AE-prothrombin was readily made refractory to the two-stage analytical reagents with purified platelet factor 3 and calcium ions. Combinations of sodium cholate and phosphatidyl serine were also effective, but either one alone was ineffective.

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