scholarly journals Heterogeneity of protein–polysaccharides of porcine articular cartilage. The chondroitin–sulphate proteins associated with collagen

1971 ◽  
Vol 123 (5) ◽  
pp. 747-755 ◽  
Author(s):  
K. D. Brandt ◽  
Helen Muir
Keyword(s):  
Articular Cartilage ◽  
Sodium Acetate ◽  
Chondroitin Sulphate ◽  
Average Length ◽  
Alkali Treatment ◽  
Molar Ratio ◽  
Sodium Acetate Solution ◽  
Acetate Solution ◽  
Keratan Sulphate ◽  
Collagenase Digestion

Pig articular cartilage, from which protein–polysaccharides soluble in iso-osmotic sodium acetate had been removed, was extracted in three further stages with 8m-urea in 2m-sodium acetate and with tris–HCl buffer after bacterial collagenase digestion, followed by the same urea–sodium acetate solution, thus leaving only 2% of the original uronic acid in the tissue. The histological appearance of the cartilage was unaltered until after collagenase digestion. The collagenase used did not affect the viscosity or molecular size of a protein–polysaccharide preparation obtained previously. The protein–polysaccharides in each extract differed in size, amino acid composition and protein content, but protein and keratan sulphate contents were not related to hydrodynamic size, in contrast with protein–polysaccharides extracted previously before collagenase digestion. Hydroxyproline could not be removed from those obtained by the first urea–sodium acetate extraction until degraded by heat. The galactosamine/pentose molar ratio agreed closely with the galactosamine/serine molar ratio that was destroyed on treatment with 0.5m-sodium hydroxide, showing that chondroitin sulphate was attached only to serine residues. From these molar ratios the chondroitin sulphate chains were calculated to be of the same average length in protein–polysaccharides in all three extracts although somewhat shorter than in protein–polysaccharides extracted previously. Some threonine residues were also destroyed on alkali treatment suggesting that keratan sulphate may be attached to threonine. These findings together with previous results show that differences in size, composition and physical state extend to all the protein–polysaccharides in cartilage.

scholarly journals Characterization of protein–polysaccharides of articular cartilage from mature and immature pigs

1969 ◽  
Vol 114 (4) ◽  
pp. 871-876 ◽  
Author(s):  
Kenneth D. Brandt ◽  
Helen Muir
Keyword(s):  
Articular Cartilage ◽  
Sodium Acetate ◽  
Chondroitin Sulphate ◽  
Average Length ◽  
Analytical Data ◽  
Age Groups ◽  
Extraction Procedure ◽  
Gel Filtration ◽  
Calcium Acetate ◽  
Keratan Sulphate

Protein–polysaccharides of femoral articular cartilage from pigs of ages 9 months and 5 weeks were compared after extraction at pH6·8 with iso-osmotic sodium acetate followed by 0·63m-calcium acetate. The cartilage from the younger animals had a higher moisture content and contained considerably larger amounts of protein–polysaccharide, but less than half as much collagen/g. dry weight, than cartilage from the older pigs. There was notably less keratan sulphate in the fractions from the less mature animals. After gel filtration on 6% agarose, elution profiles of the calcium acetate extracts were similar to those of the sodium acetate extracts of the same tissue. Chemical analyses, however, showed that in both age-groups the extraction procedure had achieved a sequential solubilization of protein–polysaccharides in that the initial extracts contained a higher proportion of keratan sulphate than those that were extracted subsequently. Both extracts from the older animals contained up to 25% of a relatively small protein–polysaccharide that was retarded on 6% agarose and that had a lower protein content and less keratan sulphate than the larger protein–polysaccharides. In contrast, in extracts from the less mature cartilage only about 5% of the protein–polysaccharides were small enough to be retarded by 6% agarose, suggesting that the small components may not be precursors of the larger. The average length of chondroitin sulphate chains, as calculated from the analytical data, was the same in the smaller protein–polysaccharides as in the larger.

scholarly journals Structure of aqueous sodium acetate solutions by X-Ray scattering and density functional theory

2020 ◽  
Vol 92 (10) ◽  
pp. 1627-1641
Author(s):  
Guangguo Wang ◽  
Yongquan Zhou ◽  
He Lin ◽  
Zhuanfang Jing ◽  
Hongyan Liu ◽  
...  
Keyword(s):  
Sodium Acetate ◽  
Density Functional ◽  
Hydration Shell ◽  
Ion Pair ◽  
Water Molecules ◽  
Sodium Acetate Solution ◽  
Acetate Solution ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

AbstractThe structure of aq. sodium acetate solution (CH3COONa, NaOAc) was studied by X-ray scattering and density function theory (DFT). For the first hydrated layer of Na+, coordination number (CN) between Na+ and O(W, I) decreases from 5.02 ± 0.85 at 0.976 mol/L to 3.62 ± 1.21 at 4.453 mol/L. The hydration of carbonyl oxygen (OC) and hydroxyl oxygen (OOC) of CH3COO− were investigated separately and the OC shows a stronger hydration bonds comparing with OOC. With concentrations increasing, the hydration shell structures of CH3COO− are not affected by the presence of large number of ions, each CH3COO− group binds about 6.23 ± 2.01 to 7.35 ± 1.73 water molecules, which indicates a relatively strong interaction between CH3COO− and water molecules. The larger uncertainty of the CN of Na+ and OC(OOC) reflects the relative looseness of Na-OC and Na-OOC ion pairs in aq. NaOAc solutions, even at the highest concentration (4.453 mol/L), suggesting the lack of contact ion pair (CIP) formation. In aq. NaOAc solutions, the so called “structure breaking” property of Na+ and CH3COO− become effective only for the second hydration sphere of bulk water. The DFT calculations of CH3COONa (H2O)n=5–7 clusters suggest that the solvent-shared ion pair (SIP) structures appear at n = 6 and become dominant at n = 7, which is well consistent with the result from X-ray scattering.

Analytical Methods for Diethylstilbestrol in Feeds and Premixes

1966 ◽  
Vol 49 (5) ◽  
pp. 895-898
Author(s):  
Loyal R Stone
Keyword(s):  
Acetic Acid ◽  
Analytical Methods ◽  
Sodium Acetate ◽  
Buffer System ◽  
Official Method ◽  
Sodium Acetate Solution ◽  
Acetate Solution ◽  
Acid Buffer System ◽  
Acetic Acid Buffer

Abstract Methods are presented in which diethylstilbestrol is extracted from feeds in the Goldfisch apparatus, transferred into alkaline sodium acetate solution to avoid emulsions, and measured colorimetrically in a sodium acetate-acetic acid buffer system. The procedure is rapid, and results agree closely with those obtained by the official method. Procedures are also presented for determination of diethylstilbestrol in molasses and fat mixtures.

The Basis of Bentazon Antagonism on Sethoxydim Absorption and Activity

Weed Science ◽  
1989 ◽  
Vol 37 (3) ◽  
pp. 400-404 ◽  
Author(s):  
Gunawan Wanamarta ◽  
Donald Penner ◽  
James J. Kells
Keyword(s):  
Sodium Salt ◽  
Sodium Acetate ◽  
Tomato Fruit ◽  
Weak Acid ◽  
Antagonistic Effect ◽  
Hydroxyl Group ◽  
Sodium Acetate Solution ◽  
Acetate Solution ◽  
Spray Solution ◽  
Leaf Surfaces

The antagonistic effect of bentazon on sethoxydim adsorption and activity was studied in quackgrass. The diffusion of14C-sethoxydim into and through an isolated tomato fruit cuticle was inhibited in the presence of the sodium salt of bentazon. Bentazon also increased the partitioning of14C-sethoxydim into CH2Cl2and water; however, it decreased partitioning into ethyl acetate. Removal of epicuticular wax from quackgrass leaf surfaces did not prevent the antagonism. Addition of sodium acetate or sodium bicarbonate to the sethoxydim spray solution at 10 mM reduced uptake of14C-sethoxydim by quackgrass similar to the effect of bentazon. Sodium ions in the bentazon formulation appeared responsible for the antagonism by exchanging with the H+of the sethoxydim hydroxyl group to form a more polar sodium salt of sethoxydim. The addition of Li+, K+, Cs+, Ca++, and Mg++cations associated with a weak acid also reduced14C-sethoxydim absorption. Addition of organic acids to the spray solution overcame the antagonism by preventing the formation of sodium salt of sethoxydim. In the field, the addition of a 3000 ppm sodium acetate solution delivering 0.56 kg/ha produced the same antagonism as bentazon on quackgrass control with sethoxydim.

scholarly journals Studies on protein–polysaccharides from pig laryngeal cartilage. Extraction and purification

1969 ◽  
Vol 113 (5) ◽  
pp. 879-884 ◽  
Author(s):  
C. P. Tsiganos ◽  
Helen Muir
Keyword(s):  
Hyaluronic Acid ◽  
Chloride Solution ◽  
Sodium Acetate ◽  
Serum Proteins ◽  
Chondroitin Sulphate ◽  
Calcium Chloride Solution ◽  
Keratan Sulphate ◽  
Laryngeal Cartilage ◽  
Extraction And Purification ◽  
Degradative Enzymes

1. Protein–polysaccharides of chondroitin sulphate were extracted from fresh laryngeal cartilage at pH6·8 by two procedures. Procedure I consisted of brief low-speed homogenization in 0·15m (iso-osmotic) sodium acetate and procedure II consisted of longer homogenization followed by prolonged extraction in 10% calcium chloride solution. 2. The protein–polysaccharides in both extracts were isolated and purified by precipitation with 9-aminoacridine hydrochloride. They were free from serum proteins, collagen and nucleic acids and also of degradative enzymes. The absence of such enzymes was shown by viscosity measurements on solutions of protein–polysaccharides incubated for up to 24hr. at pH4 and 6·8. 3. Mannose, glucose or fucose were not detected by paper chromatography and only traces of sialic acid were present. 4. The yield with procedure II was twice that with procedure I and the products differed in their protein and glucosamine contents. 5. Hyaluronic acid was unlikely to have been precipitated at an acid pH, so the glucosamine was attributed to keratan sulphate, as serum proteins were absent. There was no free keratan sulphate in the preparation. 6. Both preparations were heterogeneous in the ultracentrifuge, showing at least three components.

Studies on Iron (Fe[sup 3+]∕Fe[sup 2+])-Complex/Bromine (Br[sub 2]∕Br[sup −]) Redox Flow Cell in Sodium Acetate Solution

2006 ◽  
Vol 153 (5) ◽  
pp. A929 ◽  
Author(s):  
Y. H. Wen ◽  
H. M. Zhang ◽  
P. Qian ◽  
H. T. Zhou ◽  
P. Zhao ◽  
...  
Keyword(s):  
Sodium Acetate ◽  
Flow Cell ◽  
Sodium Acetate Solution ◽  
Acetate Solution ◽  
Redox Flow Cell

scholarly journals The alkali-labile linkage between keratan sulphate and protein

1974 ◽  
Vol 141 (1) ◽  
pp. 57-69 ◽  
Author(s):  
John J. Hopwood ◽  
H. Clem Robinson
Keyword(s):  
Intervertebral Disc ◽  
Chondroitin Sulphate ◽  
Alkali Treatment ◽  
Glycosidic Bond ◽  
Proteus Vulgaris ◽  
Keratan Sulphate ◽  
Covalently Bonded ◽  
Sequential Digestion

Keratan sulphate was isolated from adult intervertebral disc in 90% yield by sequential digestion of the whole tissue with papain, Pronase and Proteus vulgaris chondroitin sulphate lyase. Treatment of this preparation with alkali cleaved a glycosidic bond between N-acetylgalactosamine and threonine and produced, by an alkali-catalysed ‘peeling’ reaction, an unsaturated derivative of N-acetylgalactosamine which reacted as a chromogen in the Morgan–Elson reaction, but remained covalently bonded to the keratan sulphate chain. This derivative was reduced and labelled by alkaline NaB3H4. The substituent at position 3 of N-acetylgalactosamine in the keratan sulphate–protein linkage was identified as a disaccharide, N-acetylneuraminylgalactose, which was isolated from the reaction mixture after alkali treatment.

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