Volumetric Studies of Sodium Dodecyl Sulphate in Aqueous and Aqueous Amino Acid Solutions

2012 ◽  
Vol 28 (1) ◽  
pp. 165-187 ◽  
Author(s):  
Roksana Khatun ◽  
Md. Nazrul Islam
Keyword(s):  
Amino Acid ◽  
Sodium Dodecyl Sulphate ◽  
Sodium Dodecyl ◽  
Acid Solutions ◽  
Amino Acid Solutions

scholarly journals Temperature Dependence of Volumetric and Viscometric Studies on SDS in Amino Acid Solutions

2020 ◽  
Vol 63 (1) ◽  
pp. 30-39
Author(s):  
Muhammad Sarwar Hossain ◽  
Bishwajit Kumar Das ◽  
Abul Khayer Morol
Keyword(s):  
Amino Acid ◽  
Ternary System ◽  
Temperature Dependence ◽  
Butyric Acid ◽  
Sodium Dodecyl ◽  
Solvent System ◽  
Acid Solutions ◽  
Concentration Region ◽  
Amino Butyric Acid ◽  
Amino Acid Solutions

The temperature dependence studies on the binary and ternary system are very few. The densities of sodium dodecyl sulphate (SDS), L-arginine, 2-amino butyric acid in water and SDS mixed with L-arginine and 2-amino butyric acid solutions have been measured precisely at five equidistant temperatures ranging from 293.15K to 313.15K at an interval of 5K. The variety of different thermo- dynamics properties of SDS were observed in the low concentration region. The density of all the studied system was found to increase with the increase of molar concentration of the solution and decrease with the increase of temperature. SDS acts as structure breaker for both regions in aqueous L-arginine and 2-amino butyric acid solvent system at studied temperature.    

INTRAVENOUS NUTRITION WITH AMINO ACID SOLUTIONS IN PATIENTS WITH CHRONIC URAEMIA

1972 ◽  
Vol 191 (4) ◽  
pp. 359-367
Author(s):  
J. Bergström ◽  
H. Bucht ◽  
P. Fürst ◽  
E. Hultman ◽  
B. Josephson ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Solutions ◽  
Chronic Uraemia ◽  
Amino Acid Solutions ◽  
Intravenous Nutrition

scholarly journals The molybdenum–iron protein of Klebsiella pneumoniae nitrogenase. Evidence for non-identical subunits from peptide ‘mapping’

1976 ◽  
Vol 155 (2) ◽  
pp. 383-389 ◽  
Author(s):  
C Kennedy ◽  
R R. Eady ◽  
E Kondorosi ◽  
D K Rekosh
Keyword(s):  
Amino Acid ◽  
Klebsiella Pneumoniae ◽  
Sodium Dodecyl Sulphate ◽  
Azotobacter Vinelandii ◽  
Peptide Mapping ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Amino Acid Content ◽  
Rhizobium Japonicum ◽  
Fe Protein

The molybdenum- and iron-containing protein components of nitrogenase purified from Klebsiella pneumoniae, Azotobacter vinelandii, Azotobacter chroococcum and Rhizobium japonicum bacteroids all gave either one or two protein-staining bands after sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, depending on the commercial brand of sodium dodecyl sulphate used. The single band obtained with K. pneumoniae Mo-Fe protein when some commercial brands of sodium dodecyl sulphate were used in the preparation of the electrode buffer was resolved into two bands by the addition of 0.01% (v/v) dodecanol to the buffer. Protein extracted from the two bands obtained after electrophoresis of K. pneumoniae Mo-Fe protein gave unique and distinct peptide ‘maps’ after tryptic digestion. Undissociated Mo-Fe protein contained both sets of tryptic peptides. These data are consistent with Mo-Fe protein from K. pneumoniae being composed of non-identical subunits. Amino acid analyses of the subunit proteins revealed some clear differences in amino acid content, but the two subunits showed close compositional relatedness, with a different index [Metzer, H., Shapiro, M.B., Mosiman, J.E. & Vinton, J.G. (1968) Nature (London) 219, 1166-1168] of 4.7.

scholarly journals Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure

1983 ◽  
Vol 213 (1) ◽  
pp. 225-234 ◽  
Author(s):  
N Lambert ◽  
R B Freedman
Keyword(s):  
Amino Acid ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sedimentation Coefficient ◽  
Bovine Liver ◽  
Polyacrylamide Gel ◽  
Protein Disulphide Isomerase

Protein disulphide-isomerase from bovine liver was purified to homogeneity as judged by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, two-dimensional electrophoresis and N-terminal amino acid analysis. The preparative procedure, a modification of that of Carmichael, Morin & Dixon [(1977) J. Biol. Chem. 252, 7163-7167], is much faster and higher-yielding than previous procedures, and the final purified material is of higher specific activity. The enzyme has Mr 57 000 as determined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, both in the presence and in the absence of thiol compounds. Gel-filtration studies on Sephadex G-200 indicate an Mr of 107 000, suggesting that the native enzyme is a homodimer with no interchain disulphide bonds. Ultracentrifugation studies give a sedimentation coefficient of 3.5S, implying that the enzyme sediments as the monomer. The isoelectric point, in the presence of 8 M-urea, is 4.2, and some microheterogeneity is detectable. The amino acid composition is comparable with previous analyses of this enzyme from bovine liver and of other preparations of thiol:protein disulphide oxidoreductases whose relation to protein disulphide-isomerase has been controversial. The enzyme contains a very high proportion of Glx + Asx residues (27%). The N-terminal residue is His. The pure enzyme has a very small carbohydrate content, determined as 0.5-1.0% by the phenol/H2SO4 assay. Unless specific steps are taken to remove it, the purified enzyme contains a small amount (5 mol/mol of enzyme) of Triton X-100 carried through the purification.

scholarly journals An aquatic vertebrate can use amino acids from environmental water

2016 ◽  
Vol 283 (1839) ◽  
pp. 20160996 ◽  
Author(s):  
Noboru Katayama ◽  
Kobayashi Makoto ◽  
Osamu Kishida
Keyword(s):  
Amino Acids ◽  
Organic Matter ◽  
Amino Acid ◽  
Dissolved Organic Matter ◽  
Larval Growth ◽  
Environmental Water ◽  
Acid Solutions ◽  
Aquatic Vertebrates ◽  
Amino Acid Solutions ◽  
Salamander Larvae

Conventional food-web theory assumes that nutrients from dissolved organic matter are transferred to aquatic vertebrates via long nutrient pathways involving multiple eukaryotic species as intermediary nutrient transporters. Here, using larvae of the salamander Hynobius retardatus as a model system, we provide experimental evidence of a shortcut nutrient pathway by showing that H. retardatus larvae can use dissolved amino acids for their growth without eukaryotic mediation. First, to explore which amino acids can promote larval growth, we kept individual salamander larvae in one of eight different high-concentration amino acid solutions, or in control water from which all other eukaryotic organisms had been removed. We thus identified five amino acids (lysine, threonine, serine, phenylalanine, and tyrosine) as having the potential to promote larval growth. Next, using 15 N-labelled amino acid solutions, we demonstrated that nitrogen from dissolved amino acids was found in larval tissues. These results suggest that salamander larvae can take up dissolved amino acids from environmental water to use as an energy source or a growth-promoting factor. Thus, aquatic vertebrates as well as aquatic invertebrates may be able to use dissolved organic matter as a nutrient source.

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