Interaction of Some Amino Acids with Sodium Dodecyl Sulphate in Aqueous Solution at Different Temperatures

2011 ◽  
Vol 66a ◽  
pp. 339
Author(s):  
Ali A. ◽  
Itoo F. A. ◽  
Ansari N. H.
2014 ◽  
Vol 112 (20) ◽  
pp. 2681-2693 ◽  
Author(s):  
Anwar Ali ◽  
Nisar Ahmad Malik ◽  
Sahar Uzair ◽  
Maroof Ali

2011 ◽  
Vol 66 (5) ◽  
pp. 345-352
Author(s):  
Anwar Ali ◽  
Firdoos Ahmad Itoo ◽  
Nizamul Haque Ansari

The density ρ, and viscosity η of 0.00, 0.05, 0.10, 0.15, and 0.20 mol kg−1 glycine (Gly), dlalanine (Ala), dl-serine (Ser), and dl-valine (Val) have been measured in 0.002 mol kg−1 aqueous sodium dodecyl sulphate (SDS) at 298.15, 303.15, 308.15, and 313.15 K. These data have been used to calculate the apparent molar volume φv, infinite dilution apparent molar volume φv°, and the standard partial molar volumes of transfer φv° (tr), of the amino acids from water to the aqueous SDS solutions. Falkenhagen coefficient A, Jones-Dole coefficient B, free energies of activation per mole of solvent (aqueous SDS) Δμ1°*, and per mole solute (amino acids) Δμ2°*, also enthalpy ΔH* and entropy ΔS* of activation of viscous flow were evaluated using viscosity data. The molar refraction RD was calculated by using experimental values of the refractive index nD of the systems. The results have been interpreted in terms of ion-ion, ion-polar and hydrophobic-hydrophobic group interactions. The volume of the transfer data suggest that ion-ion intertactions are predominant.


2010 ◽  
Vol 2 (2) ◽  
pp. 313-321 ◽  
Author(s):  
K. M. A. Haque ◽  
M. S. Hussain

Nano-sized nickel particles have been synthesized by a bottom-up approach, using hydrazine as the reducing agent in the presence of an anionic surfactant - sodium-dodecyl sulphate (SDS). The effect of adding a nonionic polymer -polyvinylpyrrolidone (PVP) with an anionic surfactant has been studied at two different temperatures; the rate of reduction increased as the reaction temperature was increased from 60 to 100°C. These nano-aggregated nickel particles were characterized by using SEM with EDX facilities and TEM. TEM characterization showed the presence of spherical Ni particles as fine as 10nm in diameter. However, the SEM images showed a very spiky morphology, very small spherical shaped objects were clearly observed within these spiky structures. The combination of SDS/PVP reaction produced nano-sized nickel particles which were much finer than the reactions where SDS was used on its own. PVP has shown some dispersion power, and was found to be capable of preventing nickel particles from gradual agglomeration.  Keywords: Bottom-up; SDS; PVP; 10 nm. © 2010 JSR Publications. ISSN: 2070-0237 (Print); 2070-0245 (Online). All rights reserved.       DOI:10.3329/jsr.v2i2.3261               J. Sci. Res. 2 (2), 313-321 (2010) 


1971 ◽  
Vol 122 (5) ◽  
pp. 623-631 ◽  
Author(s):  
Anne M. S. Marr ◽  
A. Neuberger ◽  
Wendy A. Ratcliffe

1. Tamm–Horsfall glycoprotein from rabbit urine has been isolated and characterized. The homogeneity of the preparation has been established by a variety of procedures including disc gel electrophoresis and ultracentrifugation in aqueous solution, sodium dodecyl sulphate and formic acid. 2. The chemical composition has been determined and a carbohydrate content of approx. 31% was obtained. The relative contents of the amino acids were shown to be very similar to those in human Tamm–Horsfall glycoprotein. A trace of lipid was also detected. 3. Leucine was identified as the only N-terminal amino acid. 4. The subunit structure was investigated in the presence of sodium dodecyl sulphate by gel filtration and disc gel electrophoresis. These studies indicated that the subunit possessed a molecular weight of approx. 84000±6000. A similar value was obtained after reduction and S-alkylation of the glycoprotein indicating that the disulphide bonds were all intrachain. 5. A minimum value for the chemical molecular weight of 85000±6000 was obtained from the number of N-terminal amino acids released by cyanogen bromide cleavage of the glycoprotein. 6. The immunological properties of the glycoprotein were studied. Cross reactivity was demonstrated between human Tamm–Horsfall glycoprotein and a guinea-pig anti-rabbit Tamm–Horsfall antiserum.


1980 ◽  
Vol 193 (1) ◽  
pp. 29-36 ◽  
Author(s):  
Yoshio Kato ◽  
Katsuo Komiya ◽  
Hiroo Sasaki ◽  
Tsutomu Hashimoto

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