Volumetric, compressibility and viscometric studies on sodium cholate/sodium deoxycholate–amino acid interactions in aqueous medium

2015 ◽  
Vol 606 ◽  
pp. 12-24 ◽  
Author(s):  
Kuldeep Kumar ◽  
Suvarcha Chauhan
Keyword(s):  
Amino Acid ◽  
Aqueous Medium ◽  
Sodium Deoxycholate ◽  
Sodium Cholate

Self-Aggregation Phenomenon of Promazine Hydrochloride Under the Influence of Sodium Cholate/Sodium Deoxycholate in Aqueous Medium

2015 ◽  
Vol 37 (3) ◽  
pp. 450-463 ◽  
Author(s):  
Muhanna K. Al-Muhanna ◽  
Malik Abdul Rub ◽  
Naved Azum ◽  
Sher Bahadar Khan ◽  
Abdullah M. Asiri
Keyword(s):  
Aqueous Medium ◽  
Sodium Deoxycholate ◽  
Sodium Cholate ◽  
Self Aggregation ◽  
Aggregation Phenomenon

scholarly journals Chain Length of Amphipathic-Type Thioesters Dramatically Affects Reactivity in Aqueous Amidation Reactions with Cysteine Esters

SynOpen ◽  
2017 ◽  
Vol 01 (01) ◽  
pp. 0059-0062
Author(s):  
Ikumi Otomo ◽  
Kanna Watanabe ◽  
Chiaki Kuroda ◽  
Kenichi Kobayashi
Keyword(s):  
Amino Acid ◽  
Aqueous Medium ◽  
Chain Length ◽  
Ethyl Esters ◽  
Side Chain ◽  
Amino Acid Side Chain ◽  
Hydrophobic Properties ◽  
M 10 ◽  
Hexyl Ester ◽  
Close Proximity

The reaction of five amphipathic-type thioesters, CH3(CH2) m COS(CH2) n COONa (m + n = 12), with cysteine hexyl, butyl, and ethyl esters were studied in aqueous medium. Compounds with the thioester group in close proximity to the carboxylate moiety (m = 10, n = 2) afforded amides in almost quantitative yield, whereas no reaction proceeded by using compounds with the thioester group distant from the carboxylate. In contrast, no clear difference in yield was observed among the five amphipathic-type thioesters upon reaction with valine hexyl ester. The results indicate that the reaction is affected by both the position of the thioester group and the hydrophilic/hydrophobic properties of the amino acid side chain.

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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