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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.
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.
Induction of Nucleolin Translocation by Acharan Sulfate in A549 Human Lung Adenocarcinoma
Eun Ji Joo,Yang Hui,Youmie Park,Nam Young Park,Toshihiko Toida,Robert J. Linhardt,Yeong Shik Kim 한국당과학회 2010 한국당과학회 학술대회 Vol.2010 No.1
Acharan sulfate (AS), isolated from the giant African snail Achatina fulica, is a novel glycosaminoglycan, consisting primarily of the repeating disaccharide structure a-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 mg/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.
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>
Conjugation of Ginsenoside Rg3 with Gold Nanoparticles
박유미,A-Rang Im,Eun Ji Joo,Jihye Lee,박형근,강영화,Robert J. Linhardt,Yeong Shik Kim 대한화학회 2011 Bulletin of the Korean Chemical Society Vol.32 No.1
Ginsenoside Rg3 was reported to have important biological activities. We demonstrate conjugation and quantification procedures of ginsenoside Rg3 to gold nanoparticles for future biological and medical applications. Ginsenoside Rg3was conjugated to spherical gold nanoparticles using a bifunctional heptaethylene glycol linker. The sulfhydryl group of heptaethylene glycol was adsorbed onto gold nanoparticles, and carboxylic acid end of heptaethylene glycol was bonded through a hydroxyl group of Rg3 via ester bond formation. The conjugation of Rg3 was characterized with various spectroscopic techniques, high resolution-transmission electron microscopy, and using Rg3 monoclonal antibody. The Rg3- functionalized gold nanoparticles were 4.7 ± 1.0 nm in diameter with a surface charge of ‒4.12 mV. The total number of Rg3 molecules conjugated to a 3.6 mL solution of gold nanoparticle was determined to be 9.5 ×10^14 corresponding to ~6 molecules of Rg3/gold nanoparticle. These results suggest that ginsenoside Rg3 is successfully conjugated to gold nanoparticles via heptaethylene glycol linker. The quantification was performed by using Rg3monoclonal antibody without interference of gold’s intrinsic color.