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( Zhong Jin Qian ),( Tae Kil Eom ),( Bo Mi Ryu ),( Se Kwon Kim ) 한국키틴키토산학회 2010 한국키틴키토산학회지 Vol.15 No.2
The angiotensin I converting enzyme (ACE) inhibitory effects of three kinds of sulfated chitooligosaccharides (SCOS), relatively higher molecular weight SCOS (HMWSCOS, 5-10 kDa), medium molecular weight SCOS (MMWSCOS, 5-3 kDa), and lower molecular weight SCOS (LMWSCOS, 3-1 kDa), respectively. The MMWSCOS exhibited the higher inhibition activity with the IC50 value of 0.25mg/mL than other sulfated chitooligasaccharides (MMWSCOS: 0.775mg/mL and LMWSCOS: 0.325 mg/ml). Furthermore, all SCOSs showed no cytotoxicity on human embryonic lung fibroblast cell line (MRC-5) and Lineweaver-Burk plots suggest that MMWSCOS and LMWSCOS acts as non-competitive inhibitor to inhibit ACE. Therefore, these results exhibited that substitution of the hydrogen atom at the C-6 position of pyranose residue by the sulfate group promotes ACE inhibitory effects of COS and they would be beneficial ingredients for nutraceuticals and pharmaceuticals against hypertension and related diseases.
Isolation and Characterization of Collagen from Skin of Bullfrog, Rana catesbeiana Shaw
Qian, Zhong-Ji,Jung, Won-Kyo,Ngo, Nghiep Dai,Lee, Sang-Hoon,Kim, Se-Kwon The Korean Society of Fisheries and Aquatic Scienc 2007 Fisheries and Aquatic Sciences Vol.10 No.2
In order to utilize skin of bullfrog (Rana catesbeiana Shaw) as an alternative source of collagen, we investigated and compared biochemical and physical properties of collagens isolated from bullfrog skin. Two kinds of collagen (BSASC; bullfrog skin acid-soluble collagen and BSPSC; bullfrog skin pepsin-solubilized collagen) were isolated by subsequent treatments with acetic acid and pepsin. The amounts of skin collagen isolated in the subsequent treatments were 7.3% BSASC and 18.2% BSPSC on the basis of lyophilized bullfrog skin weight, respectively. According to the electrophoretic pattern and CM-cellulose column chromatogram, the BSASC has the chain composition of ${\alpha}1{\alpha}2{\alpha}3$ heterotrimer, and the BSPSC consists of two ${\alpha}$ chains of ${\alpha}1{\alpha}2$. In addition, the denaturation temperatures of all collagens tested were ranged from $30^{\circ}C\;to\;38^{\circ}C$. This study suggests that there is a possibility to use bullfrog skin collagen as an alternative source of collagen for industrial purposes, and subsequently it may increase the economical value of the bullfrog.
Qian, Zhong‐,Ji,Jung, Won‐,Kyo,Kang, Kyong‐,Hwa,Ryu, BoMi,Kim, Se‐,Kwon,Je, Jae‐,Young,Heo, Soo‐,Jin,Oh, Chulhong,Kang, Do‐,Hyung,Park, Won Sun,Choi, Ilȁ Blackwell Publishing Ltd 2012 Journal of phycology Vol.48 No.2
<P>Microalgae are major primary producers of organic matter in aquatic environments through their photosynthetic activities. Fermented microalga (<I>Pavlova lutheri</I> Butcher) preparation (FMP) is the product of yeast fermentation by <I>Hansenula polymorpha</I>. It was tested for the antioxidant activities including lipid peroxidation inhibitory activity, free‐radical‐scavenging activity, inhibition of reactive oxygen species (ROS) on mouse macrophages (RAW264.7 cell), and inhibited myeloperoxidase (MPO) activity in human myeloid cells (HL60). FMP exhibited the highest antioxidant activity on free‐radical scavenging, inhibitory intracellular ROS, and inhibited MPO activity. MTT [3‐(4,5‐dimethyl‐2‐yl)‐2,5‐diphenyltetrazolium bromide] assay showed no cytotoxicity in mouse macrophages (RAW264.7 cell), human myeloid cells (HL60), and human fetal lung fibroblast cell line (MRC‐5). Furthermore, the antioxidative mechanism of FMP was evaluated by protein expression levels of antioxidant enzyme (superoxide dismutase [SOD] and glutathione [GSH]) using Western blot. The results obtained in the present study indicated that FMP is a potential source of natural antioxidant.</P>