• 한국식품영양과학회지
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• 제23권6호
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• pp.945-949
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• 1994

Chondroitin sulfate (Chs) contents in edible snail , Achatina fulica Bowdich , andits processed meat extracts were determined by high-performance liquid chormatogrpahy(HPLC) and spectrophotometric method. Spectrophotometric method was based on the precipitation of acriflavine by ChS, and HPLC method was based on the detection of two unsaturated disaccharides, 2-acetamido-2-deoxy-3-O-($\beta$ -D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose($\Delta$Di-4S) and 2-acetamido-2deoxy-3-O-($\beta$-D-gluco-4-eepyranosyluronic acid)-6-O-sulfo-D-galactose ($\Delta$야-6S) librated from ChS byenzymeatic digestion with chondroitinase ABc. the ratio of 125$\mu$mol of sodium hydroxide to mg of ChS and 8$0^{\circ}C$ of reaction temperature were proper for alkaline hydrolysis to remove protein residue form ChS. In assay preparation for HPLC ethod, the iptimum concentration of the enzyme chondroitinase ABc was 0.15 unit per 50 $\mu\textrm{g}$ of ChS at a fixed reaction time (30 min) and pH 8.0 using Tris buffer. ChS content in edible snail was 177.6mg% by spectrophotometric method and 153.5mg% by HPLC method and those in the processed meat extract was 71.3mg% by spectrometric method ad 62.8mg% by HPLC method, respectively.

• 한국가금학회:학술대회논문집
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• 한국가금학회 2004년도 제21차 정기총회 및 학술발표회
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• pp.26-27
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• 2004

닭 용골연골을 이용하여 CS를 함유하는 뮤코다당단백질을 추출하는데 있어 경제성을 고려하여 최적의 조건을 조사하기 위하여 본 연구를 실시하였다. 열수 추출의 경우 120분간 추출하였을 때 그 수율과 CS 함량이 가장 효율적으로 나타났으며, 효소 추출은 2 %의 alcalase를 첨가한 후 120분 동안 추출하였을 때 수율과 CS 함량이 가장 효과적인 것으로 나타났다. CS를 다량 포함하는 정제소재를 제조하기 위해 ethanol 침전을 실시한 결과. 수율은 21.41 %, CS 함량은 46.31 %로 나타났다.

• Archives of Pharmacal Research
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• 제27권8호
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• pp.867-872
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• 2004

Oxidative stress due to reactive oxygen species (ROS) can cause oxidative damage to cells. Cells have a number of defense mechanisms to protect themselves from the toxicity of ROS. Mitochondria are especially important in the oxidative stress as ROS have been found to be constantly generated as an endogen threat. Mitochondrial defense depends mainly on super-oxide dismutase (SOD) and glutathione peroxidase (GPx), whereas microsomal defense depends on catalase (CAT), which is an enzyme abundant in microsomes. SOD removes superoxide anions by converting them to $H_2O$$_2$, which can be rapidly converted to water by CAT and GPx. Also, GPx converts hydroperoxide (ROOH) into oxidized-glutathione (GSSG). Ovariectomized (OVX) rats are used as an oxidative stress model. An ovariectomy increased the levels of MDA, one of the end-products in the lipid peroxidative process, and decreased levels of the antioxidative enzymes； SOD, CAT and GPx. However, Chondroitin sulfate (CS) decreased the levels of MDA, but increased the levels of SOD, CAT and GPx in a dose-depen-dent manner. Moreover, inflammation and cirrhosis of liver tissue in CS- treated rats were sig-nificantly decreased. These results suggest that CS might be a potential candidate as an anti oxidative reagent.

• Food Science and Biotechnology
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• 제14권5호
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• pp.651-655
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• 2005

Enzymatic hydrolysis of shark (Squatina oculata) cartilage (SC) was optimized by response surface methodology (RSM) for chondroitin sulfate (CS) preparation. Among 11 commercial proteases, Maxazyme NNP showed highest productivity (CS yield per enzyme cost) of CS. Optimal hydrolysis conditions determined by RSM were 1.63% and 2.87 hr for enzyme concentration and hydrolysis time ($r^2\;=\;0.9527$, p<0.0l), respectively and highest yield of hydrolysate under the conditions was 42.3%. The yield ($43.1{\pm}2.1%$) and CS content ($24.8{\pm}0.1%$) of hydrolysate at optimal condition verified statistical optimization of SC enzymatic hydrolysis was valid.

• Journal of Pharmaceutical Investigation
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• 제26권4호
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• pp.273-280
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• 1996

Chondroitin sulfate/gelatin microspheres containing dexamethasone 21-acetate were prepared by complex coacervation method and their release patterns were examined in vitro. Microspheres prepared with a small amount of crosslinking agent had smooth surface and few pores, but those with a large amount of crosslinking agent were more porous and less spherical. In vitro release patterns were varied by changing polymer/drug weight ratio and amount of crosslinking agent. The release rate of dexamethasone 21-acetate in the presence of collagenase was faster than that in the absence of collagenase. Anti-inflammatory effect of dexamethasone 21-acetate microspheres was more efficient than that of dexamethasone 21-acetate solution in carrageenan-induced arthritis in the rat. On the basis of the above results, we might expect the degradation and drug release rate of these microspheres to be regulated by the degree of crosslinking and the level of enzymes. In patients with severe rheumatoid arthritis who have high concentration of collagenase, more drug would be released from the microspheres. An intra-articular injection therapy of rheumatoid arthritis with desired release kinetics could be developed to enhance patient compliance and therapeutic index.

• Archives of Pharmacal Research
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• 제23권2호
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• pp.182-186
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• 2000

Chondroitin sulfates proteoglycans were isolated from human placenta. For the identification of enzymatic digestion products of isolated proteoglycan, strong anion exchange-high performance liquid chromatography (SAX-HPLC) was performed. By the action of chondroitin ABC and chondroitin B lyase, three unsaturated disaccharides 2-acetamide-2-deoxy-3-O-($\beta$-D-gluco-4-enepyranosyluronic acid)-D-galactose ($\delta$Di-OS), 2-acetamide-2-deoxy-3-O-($\beta$-D-gluco-4-enepyranosyluronic acid)-6-O-su lfo-D-galactose ($\delta$Di-6S) and 2-acetamide-2-deoxy-3-O-($\beta$-D-gl uco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose ($\delta$Di-4S) were produced from the human placenta proteoglycan. The anticoagulant activity of chondroitin sulfate proteoglycan was evaluated by activated partial thromboplastin time (aPTT) assay and thrombin time (TT) assay. The clotting times of aPTT and TT were increased from 72 to 144 sec and 19 to 27 sec, respectively. The Immune-modulating activity of chondroitin sulfate proteoglycan was examined by cell proliferation assay and these results suggest that it may play a role in suppression of the function of immune-related cells.

• Archives of Pharmacal Research
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• 제21권5호
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• pp.555-558
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• 1998

chondroitin sulfates were isolated from the mud snail. For the quantitative analysis of enzymatic digestion products of isolated chondroitin sulfates, strong anion exchange-high performance liquid chromatography (SAX-HPLC) was performed. by the action of chondroitinase ABC, three unsaturated disaccharides$ 2-acetamide-2-deoxy-3-O-({\beta}-D-gluco-4-enepyranosyluronic acid)-D-galactose $$({\Delta}Di-OS), $2-acetamide-2-deoxy-3-O-({\beta}-D-gluco-4-enepyranosyluronic acid)-6-O-sulfo-D-galactose ({\Delta}Di-6S) and 2-acetamide-2-deoxy-3-O-({\beta}-D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose ({\Delta}Di-4S)$ were produced from the mud snail chondroitin sulfates. The analysis showed that relative proportion of ${\Delta}Di-OS/{\Delta}Di-6S/{\Delta}Di-4S$ was 58.7/3.1/38.2. The immunomodulating activity of chondroitin sulfate was examined by cell proliferation assay and these results suggest that it might be a immunosuppressant.

• 한국임상수의학회지
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• 제24권3호
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• pp.379-383
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• 2007

This study was performed to compare the effects of carboxymethylcellulose (CMCE), chondroitin sulfate (Chondron), and carboxymethylchitosan (CMCH) on preventing intraperitoneal adhesion. As a result, the tensile strength of adhesions formed between the parietal peritoneum and the ileal serosa was significantly decreased in the groups of three different kinds of anti-adhesive agents. The distance of adhesion site was slightly increased in the treatment groups comparing control group. In the CMCH group, the inflammatory cell infiltration, collagen hyperplasia, and neovascularization were significantly lower than those of control group. It was observed that the damage at intestinal serosa was significantly decreased in the chondron and CMCH groups comparing control group. Therefore CMCH may be useful as a anti-adhesive agent in the prevention of intraperitoneal adhesion in rats.

• 한국당과학회:학술대회논문집
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• 한국당과학회 2006년도 제1회 연례학술대회
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• pp.57-57
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• 2006

• 한국생명과학회:학술대회논문집
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• 한국생명과학회 2001년도 10주년 기념 국제학술 심포지움 및 추계학술대회
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• pp.126-126
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• 2001