Analysis Of Chondroitin Sulfate Research Articles

THERMAL DESTRUCTION OF CHONDROITIN SULPHATE ISOLATED FROM BARENTS SEA HYDROBIONTS

The results of the thermogravimetric analysis of chondroitin sulfate, isolated from the cartilage of salmon, the northern slope, and the blackmouth shark in the temperature range of 40-600 °С are shown. Thermal analysis was performed using differential thermogravimetry and differential scanning calorimetry. The crystallinity degree of the samples was evaluated using diffraction patterns. It was shown, that under experimental conditions, thermal decomposition of the bulk of chondroitin sulfate samples is observed at a temperature of 230 to 530 °C. Differential thermogravimetric curves and differential scanning calorimetry curves contain five endothermic peaks associated with desorption of physically present water. Desorption of bound water occurs almost to a temperature of 150–200 °C, which can be explained by the difficulty of breaking hydrogen bonds between water molecules and polar functional groups of chondroitin sulfate. Small endothermic peaks correspond to the process of removal the physical volume of water. Four consecutive exothermic peaks are associated with the thermal destruction of the acid, pyranose, and finally, residual carbon and sulfur compounds. The rates of mass loss at each site were determined and the activation energies of each event were calculated. The nature of the cartilage tissue from which chondroitin sulfate is extracted affects the rate of destruction. So, in the temperature range of 236-244 °С, the lowest rate of destruction is observed for XC samples isolated from salmon cartilage tissue. The effect of crystallinity degree on the process of thermal destruction of chondroitin sulfate samples is shown. The results of the thermal destruction of chitin / chitosan obtained from the northern shrimp are presented. It was found that less activation energy is required for thermal destruction of chondroitin sulfate compared to chitin/chitosan at all stages.

Extraction, Isolation and Analysis of Chondroitin Sulphate from Chicken Shank by Spectrophotometric Method

This study evaluated Chondroitin sulphate isolated from chicken shank cartilage in aspects such as sufficient quantities and requisite quality for feasible source of Chondroitin sulphate. Chondroitin sulphate has been widely used in treatment of osteoarthritis. Chondroitin sulphate not only reduces joint pain, but also inhibiting the disease progression. Chondroitin sulphate was obtained from cartilage of chicken shank, using enzyme (papain), acid (acetic acid), and heat. The cartilage obtained from chicken shank was hydrolysed using papain for 24h. Extraction was carried out using acetic acid and incubated at pH 4.5 and 37°C for 6h and 8h. The supernatan was treated with cetylpyridinium chloride (CPC), NaCl, methanol and ethanol. The precipitate obtained from extraction was dried in oven at 55°C.Chondroitin sulphate yield from 6h incubation was 16.30% and from 8h incubation was 36.35 % (dry weight). The FT-IR spectra of extracted Chondroitin sulphate was identical with Chondroitin sulphate standard (Fenchem Biotek Ltd). Overlay of the spectras showed characteristic absorption at the wave number 854.64 cm-1 for sample and 856.54 cm-1 for standard chondroitin sulphate. Quantitative analysis was performed using spectrophotometry. The precision was good with RSD <7.3% and the accuration was good with recovery of 82.48-108.88%.The detection limit and quantification limit were 0.15 ppm and 0.46 ppm. This study shows that chicken shank cartilage produces a source for isolation of chondroitin sulphate of 36.35% (dry weight) and purity of 87.87%.

Analysis of chondroitin sulfate from different sources of cartilage by electrophoretically mediated microanalysis

An electrophoretically mediated microanalysis protocol for the determination of different chondroitin sulfate origins was developed.

Extraction, isolation and analysis of chondroitin sulfate from broiler chicken biomass

This study was undertaken to investigate whether chondroitin sulfate (CS) can be efficiently isolated from broiler chicken by-product from mechanical deboning (BMD), which is a mixture of crushed bone, cartilage, skin, adipose tissue and muscle. With BMD as a starting material, it may be possible to maximize CS production from chicken cartilage. CS was liberated from BMD by proteolysis using proteolytic activities from papain, pancreatin, kiwi fruits and flavourzyme. The final product isolated by anion-exchange chromatography and differential precipitation with varying concentrations of ethanol contained CS-peptides with glucuronosyl-N-acetylgalactosamine-4-sulfate as a predominant disaccharide. All the enzyme sources used had sufficient activities to produce CS-peptides with undetectable amount of glucosamine. However, the size of peptide attaching to CS chain and the antigenicity to anti-keratan sulfate (KS) monoclonal antibody varied among the CS-peptides prepared with different proteinases. Papain digestion resulted in the smallest size of peptide with no detectable antigenicity to the anti-KS antibody. In contrast, pancreatin digestion provided CS-peptide having a very weak but positive antigenicity to the anti-KS antibody, which was much lower than that seen with CS-peptide prepared with kiwi fruit proteinase or flavourzyme. Pancreatin is suggested as an economical source of proteinase to liberate CS-peptides from BMD.

Recent Advances in the Bioactivities and Structural Analysis of Chondroitin Sulfate

Recent research data on chondroitin sulfate have suggested that they have many new biological functions such as anti-atherogenesis, anticoagulation, prevention and cure of arthritis, protection and repair of neuron during CNS development, morphogenesis and cell division. They are widely applied to functional food, clinical medicine and biomaterial. However, these bioactivities and applications are dependent on their fine structure with different monosaccharide unit and sulfation patterns. This review provides information on intimate relationship between these biological functions and the structure. Moreover, we overviewed the newly analytical methods about the composition and fine structure of them, including chromatometry, high performance liquid chromatography, mass spectrum and nuclear magnetic resonance before and after enzymolysis.

Analysis of Chondroitin Sulfate in Lumbar Intervertebral Discs at Two Different Stages of Degeneration as Assessed by Discogram

Previous studies have presented evidence that an underlying cause of intervertebral disc degeneration is related to changes in the sulfation of the proteoglycans. The sulfation of the chondroitin in cadaveric lumbar intervertebral discs, at two different stages of degeneration as assessed by discogram, were analyzed. Fourteen of 28 lumbar discs were graded 2 and the other 14 were graded 4 (i.e., more degenerated). From each disc, six regional segments were carefully isolated. Proteoglycans were solubilized from the disc tissue with 4 M GuHCl. Chondroitin sulfate chains were analyzed by diethylaminoethyl (DEAE)-Sephacel and high-performance liquid chromatography (HPLC) anion exchange chromatography. The major differences in sulfation of the chondroitin between grade 2 and grade 4 discs only occurred in the posterior central annulus and nucleus segments. The chondroitin in the posterior central nucleus segments of the grade 2 and grade 4 intervertebral discs were undersulfated as compared with the other segments, and the differences between these segments and the others were more accentuated in the grade 4 discs than in grade 2 discs.

Analysis of chondroitin sulfates in human urinary trypsin inhibitor.

A proteoglycan (PG) was separated from human urine by ion chromatography and gel filtration. With our sensitive determination method, the PG (M.W. Ca. 67, 000) was found to contain low-sulfated chondroitin 4-sulfate (Ch4S). The PG inhibited trypsin and had the same chromatographic behavior as human urinary trypsin inhibitor (HUTI), which also contained the low-sulfated Ch4S. From these results, it was concluded that the PG and HUTI were the same substance. The difference between individuals in the composition of the low-sulfated Ch4S in HUTI was also examined.

Differences in the content of chondroitin sulfate C and chondroitin sulfate A in the epiphysial growth cartilages of human vertebrae and long bones

The analysis of chondroitin sulfates from the epiphysial growth cartilages of vertebral bodies and long bones from 5 subjects is reported. The cartilages from the vertebral bodies contain an average of 77% of chondroitin sulfate C and 23% of chondroitin sulfate A, whereas cartilages from long bones (femur and humerus) contain an average of 41% of chondroitin sulfate C and 59% of chondroitin sulfate A. These results are correlated with a chemical defect of chondroitin sulfate C in a new mucopolysaccharidosis characterized by platyspondyly (flat vertebrae).