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형광기 - 기질 결합체를 이용해 폴리아크릴아미드겔 위에서 chitinase 활성의 검정
김영식,이경복,Robert J . Linhardt ( Yeong Shik Kim,Kyung Bok Lee,Robert J . Linhardt ) 생화학분자생물학회 1991 BMB Reports Vol.24 No.5
Gradient polyacrylamide gel electrophoresis was used to analyze the products formed by chitinases acting on N-acetylchitohexaose-fluorescent conjugate. N-Acetylchitooligosaccharides were conjugated to 7-amino-1,3-naphthalene disulfonic acid by reductive amination. Each oligosaccharide-fluorescent conjugate was purified by preparative gradient polyacrylamide gel electrophoresis, semi-dry electrotransfer to a positively-charged nylon membrane and recovered by washing the membrane with salt solution. N-Acetylchitohexaose-fluorescent conjugate and chitohexaose were exhaustively treated with three kinds of chitinases from Serratia marcescens, Streptomyces griseus, and green onin (Allium fistulosum L.). The bands were visualized under long wavelength of UV light. Analysis of reaction products provided the information on the action of chitinase action from different sources.
Solakyildirim, Kemal,Li, Lingyun,Linhardt, Robert J. Korean Society for Mass Spectrometry 2018 Mass spectrometry letters Vol.9 No.3
Alkaline phosphatase (AP) is a membrane-bound glycoprotein that is widely distributed in the plasma membrane of cells of various organs and also found in many organisms from bacteria to humans. The complete amino acid sequence and three-dimensional structure of human placental alkaline phosphatase have been reported. Based on the literature data, AP consists of two presumptive glycosylation sites, at Asn-144 and Asn-271. However, it only contains a single occupied N-linked glycosylation site and no occupied O-linked glycosylation sites. Hydrophilic interaction chromatography (HILIC) has been primarily employed for the characterization of the glycan structures derived from glycoproteins. N-glycan structures from human placental alkaline phosphatase (PLAP) were investigated using HILIC-Orbitrap MS, and subsequent data processing and glycan assignment software. 16 structures including 10 sialylated N-glycans were identified from PLAP.
( Kemal Solakyildirim ),( Lingyun Li ),( Robert J. Linhardt ) 한국질량분석학회 2018 Mass spectrometry letters Vol.9 No.3
Alkaline phosphatase (AP) is a membrane-bound glycoprotein that is widely distributed in the plasma membrane of cells of various organs and also found in many organisms from bacteria to humans. The complete amino acid sequence and three-dimensional structure of human placental alkaline phosphatase have been reported. Based on the literature data, AP consists of two presumptive glycosylation sites, at Asn-144 and Asn-271. However, it only contains a single occupied N-linked glycosylation site and no occupied O-linked glycosylation sites. Hydrophilic interaction chromatography (HILIC) has been primarily employed for the characterization of the glycan structures derived from glycoproteins. N-glycan structures from human placental alkaline phosphatase (PLAP) were investigated using HILIC-Orbitrap MS, and subsequent data processing and glycan assignment software. 16 structures including 10 sialylated N-glycans were identified from PLAP.
Induction of nucleolin translocation by acharan sulfate in A549 human lung adenocarcinoma
Joo, Eun Ji,Yang, Hui,Park, Youmie,Park, Nam Young,Toida, Toshihiko,Linhardt, Robert J.,Kim, Yeong Shik Wiley Subscription Services, Inc., A Wiley Company 2010 Journal of cellular biochemistry Vol.110 No.5
<P>Acharan sulfate (AS), isolated from the giant African snail Achatina fulica, is a novel glycosaminoglycan, consisting primarily of the repeating disaccharide structure α-D-N-acetylglucosaminyl (1 → 4) 2-sulfoiduronic acid. AS shows anti-tumor activity in vitro and in vivo. Despite this activity, AS is only weakly cytotoxic towards cancer cells. We examine the interactions between AS and cell-surface proteins in an effort to explain this anti-tumor activity. Using flow cytometry and affinity column chromatography, we confirm that AS has strong affinity to specific cell-surface proteins including nucleolin (NL) in A549 human lung adenocarcinomas. Surprisingly, we found the translocation of NL from nucleus to cytoplasm under the stimulation of AS (100 µg/ml) in vitro. Also, as NL exits the nucleus, the levels of growth factors such as bFGF and signaling cascade proteins, such as p38, p53, and pERK, are altered. These results suggest that the communication between AS and NL plays a critical role on signal transduction in tumor inhibition. J. Cell. Biochem. 110: 1272–1278, 2010. Published 2010 Wiley-Liss, Inc.</P>
Enhancement of Heparin and Heparin Disaccharide Absorption by the Phytolacca americana Saponins
Cho, So-Yean,Sim, Joon-Soo,Kang, Sam-Sik,Jeong, Choon-Sik,Linhardt, Robert-J,Kim, Yeong-Shik The Pharmaceutical Society of Korea 2003 Archives of Pharmacal Research Vol.26 No.12
We studied the effects of phytolaccosides, saponins from Phytolacca americana, on the intestinal absorption of heparin in vitro and in vivo. The absorption enhancing activity of these compounds (phytolaccosides B, $D_2$, E, F, G and I) was determined by changes in transepithelial electrical resistance (TEER) and the transport amount of heparin disaccharide, the major repeating unit of heparin, across Caco-2 cell monolayers. With the exception of phytolaccoside G, all of them decreased TEER values and increased the permeability in a dose-dependent and time-dependent manner. In vitro, phytolaccosides B,$D_2$, and E showed significant absorption enhancing activities, while effects by phytolaccoside F and I were mild. In vivo, phytolaccoside E increased the activated partial thromboplastin time (APTT) and thrombin time, indicating that phytolaccoside E modulated the transport of heparin in intestinal route. Our results suggest that a series of phytolaccosides from Phytolacca americana can be applied as pharmaceutical excipients to improve the permeability of macromolecules and hydrophilic drugs having difficulty in absorption across the intestinal epithelium.
Park, Y.,Hong, Y. N.,Weyers, A.,Kim, Y. S.,Linhardt, R. J. IET 2011 IET nanobiotechnology Vol.5 No.3
<P>Currently, sustainability initiatives that use green chemistry to improve and/or protect our global environment are becoming focal issues in many fields of research. Instead of using toxic chemicals for the reduction and stabilisation of metallic nanoparticles, the use of various biological entities has received considerable attention in the field of nanobiotechnology. Among the many possible natural products, polysaccharides and biologically active plant products represent excellent scaffolds for this purpose. Polysaccharides have hydroxyl groups, a hemiacetal reducing end, and other functionalities that can play important roles in both the reduction and the stabilisation of metallic nanoparticles. Among the various categories of compounds in plants that have potent biological activities, phytochemicals are emerging as an important natural resource for the synthesis of metallic nanoparticles. The focus of this review is the application of polysaccharides and phytochemicals in the green synthesis of gold and silver nanoparticles to afford biocomposites with novel uses in nanomedicine and as nanocomposites.</P>