• Title, Summary, Keyword: carbohydrate moiety

Search Result 34, Processing Time 0.035 seconds

The Glycopeptide, a Promoter of Thymidine Uptake, from Aloe Vera

  • Yang, Mi-Rim;Kang, Chun-Geun;Roh, Yeon-Suk;Son, Byeng-Wha;Choi, Hong-Dae;Park, Young-In;Lee, Seung-Ki;Choi, Sung-Won;Chung, Myung-Hee
    • Natural Product Sciences
    • /
    • v.4 no.2
    • /
    • pp.62-67
    • /
    • 1998
  • As a part of search for new biologically active constituents from aloe, we have isolated a glycopeptide, called G1G1M1DI2, from the gel(G1) of Aloe vera. Chemical and spectroscopic evidence indicated that G1G1M1DI2 is a glycopeptide. The molecular weight of G1G1M1DI2 was about 5,500 daltons, and the carbohydrate and protein contents were 20.9% and 32.6%, respectively. Periodate oxidation and enzymic degradation gave peptide moiety and carbohydrate moiety, respectively. Carbohydrate moiety is composed of fucose, galactose, glucose and mannose in a molar ratio of 0.5:2.4;48.8:48.3. Peptide moiety is composed of fifteen amino acids, and glutamic acid and glycine were the major componants. The glycopeptide, G1G1M1DI2, stimulated thymidine uptake of SCC 13 cells about 6.5 times the control. This result suggests that this glycopeptide has a skin cell proliferating activity.

  • PDF

Purification of a major protein with physiological activities from Panax ginseng C. A. Meyer (고려인삼(Panax ginseng C. A. Meyer)에서 생리활성을 보이는 25 kDa 주요단백질 (GMP)의 분리정제)

  • Kwon, Taek-H.;Oh, Sei-R.;Park, H.;Kim, Kyung-H.
    • Applied Biological Chemistry
    • /
    • v.41 no.6
    • /
    • pp.410-413
    • /
    • 1998
  • The major protein (GMP) from the roots of Panax ginseng C. A. Meyer was purified, using gel filtration and ion exchange chromatography followed by reversed-phase and ion exchange FPLC. Staining analysis indicated that the protein has a carbohydrate moiety, which was also shown by band shift experiments using various glycosidases. Electrophoretic and gel permeation studies showed that GMP has an apparent molecular weight of 63 kDa composed of possibly two subunits of 25 kDa containing carbohydrate moiety. GMP showed an anticomplementary activity on the hemolysis of red blood cells, which is a screening tool for inflammation mediator search.

  • PDF

Ionizing Radiation Effect on the Carbohydrate Moiety of Chicken Ovomucoid (계란 ovomucoid의 탄수화물 부분에 미치는 이온화방사선의 영향)

  • Lee, Young-Keun;Kim, Jin-Kyu;Kim, Jae-Sung;Song, Hi-Sup;Charoen, Saovapong;Amornraksa, Kitti
    • Journal of Radiation Protection and Research
    • /
    • v.22 no.1
    • /
    • pp.23-27
    • /
    • 1997
  • Radiation effects on carbohydrate moiety of chicken ovomucoid, a protease inhibitor as a typical allergenic glycoprotein of egg white, was observed. The trypsin inhibitory activity of chicken ovomucoid decreased exponentially and the inactivation was more significant irradiated in $N_2$ than in $O_2$. From the protein blotting, radiation caused protein degradation in $O_2$ and protein aggregation also in $N_2$. The patterns of carbohydrate blotting were also similar with that of protein blotting. Sugar chains in low molecular weight fraction (MW<5,000) were released by radiation and those in $O_2$ were higher than in $N_2$. From the HPLC patterns of the degradation of sugar chains, all peaks of oligosaccharides have the tendency to decrease with the increase of radiation dose and more remarkable in $O_2$ than in $N_2$. These results suggest that ionising radiation could cause the overall conformational changes of ovomucoid by the degradation and release of oligosaccharides.

  • PDF

Conformational Analysis of Trimannoside and Bisected Trimannoside Using Aqueous Molecular Dynamics Simulations

  • Kim, Hyun-Myung;Choi, Young-Jin;Lee, Jong-Hyun;Jeong, Karp-Joo;Jung, Seun-Ho
    • Bulletin of the Korean Chemical Society
    • /
    • v.30 no.11
    • /
    • pp.2723-2728
    • /
    • 2009
  • The conformational properties of oligosaccharides are important to understand carbohydrate-protein interactions. A trimannoside, methyl 3,6-di-O-($\alpha$-D-Man)-$\alpha$-D-Man (TRIMAN) is a basic unit of N-linked oligosaccharides. This TRIMAN moiety was further modified by GlcNAc (BISECT), which is important to biological activity of N-glycan. To characterize the trimannoside and its bisecting one we performed a molecular dynamics simulation in water. The resulting models show the conformational transition with two major and minor conformations. The major conformational transition results from the $\omega$ angle transition; another minor transition is due to the $\psi$ angle transition of $\alpha$ (1 $\rightarrow$ 6) linkage. The introduction of bisecting GlcNAc on TRIMAN made the different population of the major and minor conformations of the TRIMAN moiety. Omega ($\omega$) angle distribution is largely changed and the population of gt conformation is increased in BISECT oligosaccharide. The inter-residue hydrogen bonds and water bridges via bisecting GlcNAc residue make alterations on the local and overall conformation of TRIMAN moiety. These changes of conformational distribution for TRIMAN moiety can affect the overall conformation of N-glycan and the biological activity of glycoprotein.

Development of New Dihydropyran Linker for Solid-Phase Reaction

  • Ryu, Joon-Hyung;Jeong, Jin-Hyun
    • Archives of Pharmacal Research
    • /
    • v.22 no.6
    • /
    • pp.585-591
    • /
    • 1999
  • The linker which plays a role in connecting a polymer with a scaffold has become an important part n solid-phase reaction. To develop a new linker for alcohols and carbohydrates, dihydropyran moiety was selected in this study. New linker, 1-($4^{l},5^{l}$-dihydro-5H-pyranyl)-7-hydroxyheptan-3-one (5) was synthesized via four steps from $\delta$-valerolactone. This can be called as DDHP-linked Wang resin due to double dihy-dropyran rings. To the one pyran ring of new linker 5 was added Wang resin and other alcohols and carbohydrates as scaffolds were then added successfully to the another pyran ring. Carbohydrate and hydroxyl resins were connected via new linker in a 70% loading yield. The detachment of glucose moiety in the presence of PPTS (2 equiv.) in 1:1 n-buteanol/1,2-dichloroethane at $60^{\circ}C$ for 12 h was carried out quantitatively. When certain combinatorial chemical works are carried out using this dihydropyran linker, Wang resin itself can be recovered. Its fact is particularly very important in industry, because recovered resins can be recycled.

  • PDF

Chemical Compositions of Glycoprotein and Chondroitin Sulfates from Sea Cucumber(Stichopus japonicus) (해산 극피동물 중의 당단백질의 특성과 이용 I. 해삼 당단백질 및 황산콘드로이친의 화학조성과 특성)

  • 류홍수;문정혜;서재수
    • Journal of the Korean Society of Food Science and Nutrition
    • /
    • v.26 no.1
    • /
    • pp.72-80
    • /
    • 1997
  • To elucidate food value and medicinal effect of sea cucumbers, sugar composition of those gly-coprotein and chondroitin sulfate was studied. The contents of sulfate esters in sea cucumbers were 1.21%(blue), 0.90%(red) and 1.19%(black). Predominant carbohydrates were identified as fucose, glucose, D-mannuronic acid and N-acetylglucosamine, and those amount was more than 80% to total carbo-hydrate, while the minor sugar composition was ribose, mannose, galactose, N-acetylgalactosamine and D-glucuronic acid. Also, the major carbohydrate moiety of glycoproteins of sea cucumbers was revealed as fucose, mannose, N-acetylglucosamine, glucose and ribose, and those amount was more than 86% to total carbohydrate. Galactose, N-acetylgalactosamine, D-glucuronic acid and mannuronic acid were minor carbohydrate moiety. The contents of sulfate esters in glycoproteins were 0.96% for blue sea cucumber, 1.15% for red sea cucumber and 1.13% for black sea cucumber, while those in chondroitin sulfates were 3.52%(blue), 3.60%(red) and 3.72%(black). The carbohydrate moiety of chondroitin sulfate was identified as N-acetylgalactosamine (73~ 87%), fucose (7~15%) and D-glucuronic acid(5~12%). As the base on the IR spectrum of strong absorption appeared in 1240$cm^{-1}$ / for stretching vibrations in S=0 group and weak absorptions in 850$cm^{-1}$ / and 820$cm^{-1}$ /for stretching vibrations in C-0-S group, chondroitin sulfates had sulfate group which was bound to $C_4$in fucose.

  • PDF

A Role for the Carbohydrate Portion of Ginsenoside Rg3 in Na+ Channel Inhibition

  • Kim, Jong-Hoon;Hong, Yoon-Hee;Lee, Jun-Ho;Kim, Dong-Hyun;Nam, Ghilsoo;Jeong, Sang Min;Lee, Byung-Hwan;Lee, Sang-Mok;Nah, Seung-Yeol
    • Molecules and Cells
    • /
    • v.19 no.1
    • /
    • pp.137-142
    • /
    • 2005
  • We showed recently that ginsenosides inhibit the activity of various types of ion channel. Here we have investigated the role of the carbohydrate component of ginsenoside $Rg_3$ in the inhibition of $Na^+$ channels. The channels were expressed in Xenopus oocytes by injecting cRNAs encoding rat brain Nav1.2 ${\alpha}$ and ${\beta}1$ subunits, and analyzed by the two-electrode voltage clamp technique. Treatment with $Rg_3$ reversibly inhibited the inward $Na^+$ peak current ($I_{Na}$) with an $IC_{50}$ of $32.2{\pm}4.5{\mu}M$, and the inhibition was voltage-dependent. To examine the role of the sugar moiety, we prepared a straight chain form of the second glucose and a conjugate of this glucose with 3-(4-hydroxyphenyl) propionic acid hydrazide (HPPH). Neither derivative inhibited $I_{Na}$. Treatment with the carbohydrate portion of ginsenoside $Rg_3$, sophorose [${\beta}-D-glucopyranosyl$ ($1{\rightarrow}2$)-${\beta}-glucopyranoside$], or the aglycone (protopanaxadiol), on their own or in combination had no effect on $I_{Na}$. These observations indicate that the carbohydrate portion of ginsenoside $Rg_3$ plays an important role in its effect on the $Na^+$ channel.

Crystal Structure of Hypothetical Fructose-Specific EIIB from Escherichia coli

  • Park, Jimin;Kim, Mi-Sun;Joo, Keehyung;Jhon, Gil-Ja;Berry, Edward A.;Lee, Jooyoung;Shin, Dong Hae
    • Molecules and Cells
    • /
    • v.39 no.6
    • /
    • pp.495-500
    • /
    • 2016
  • We have solved the crystal structure of a predicted fructose-specific enzyme $IIB^{fruc}$ from Escherichia coli ($EcEIIB^{fruc}$) involved in the phosphoenolpyruvate-carbohydrate phosphotransferase system transferring carbohydrates across the cytoplasmic membrane. $EcEIIB^{fruc}$ belongs to a sequence family with more than 5,000 sequence homologues with 25-99% amino-acid sequence identity. It reveals a conventional Rossmann-like ${\alpha}-{\beta}-{\alpha}$ sandwich fold with a unique ${\beta}$-sheet topology. Its C-terminus is longer than its closest relatives and forms an additional ${\beta}$-strand whereas the shorter C-terminus is random coil in the relatives. Interestingly, its core structure is similar to that of enzyme $IIB^{cellobiose}$ from E. coli ($EcIIB^{cel}$) transferring a phosphate moiety. In the active site of the closest $EcEIIB^{fruc}$ homologues, a unique motif CXXGXAHT comprising a P-loop like architecture including a histidine residue is found. The conserved cysteine on this loop may be deprotonated to act as a nucleophile similar to that of $EcIIB^{cel}$. The conserved histidine residue is presumed to bind the negatively charged phosphate. Therefore, we propose that the catalytic mechanism of $EcEIIB^{fruc}$ is similar to that of $EcIIB^{cel}$ transferring phosphoryl moiety to a specific carbohydrate.

Characterization of Exopolysaccharides Produced by Submerged Culture of an Entomopathogenic Fungus Paecilomyces sinclairii by Using a Multi-Angle Laser Light Scattering System

  • KIM SANG-WOO;HWANG HYE-JIN;CHOI JANG-WON;YUN JONG-WON
    • Journal of Microbiology and Biotechnology
    • /
    • v.15 no.3
    • /
    • pp.560-567
    • /
    • 2005
  • Three groups of exopolysaccharides (EPSs) (designated as Fr-I, Fr-II, and Fr-III) were isolated from the culture filtrates of Paecilomyces sinclairii by gel filtration chromatography on Sepharose CL-4B. Their molecular characteristics were examined by multi-angle laser light scattering (MALLS) connected online to a size exclusion chromatography (SEC) and refractive index (RI) detector system. The weight-average molar mass of Fr-I, Fr-II, and Fr-III of EPSs were determined to be $1.540{\times}10^6,\;6.302{\times}10^4$, and $9.389{\times}10^4\;g/mol$, respectively. All three EPSs showed a fairly low polydispersity indice, ranging from 1.008 to 1.059 (nearly mono disperse behavior), and showed different carbohydrates and amino acids compositions; all fractions of EPSs consisted of mainly cystine, valine, and arginine in the protein moiety, and mainly ribose, galactose, and glucose in the carbohydrate moiety. The determination of gyration radii of the EPSs in SEC/MALLS analysis revealed the molecular shape of the Fr-I to be a rod-like structure, whereas the Fr-II and Fr-III had a random-coil structure in an aqueous solution.

Structure Determination of Sucrose by Acetylation and Acid Hydrolysis

  • Min, Hee-Jeong;Lee, Tae-Seong;Bae, Young-Soo
    • Journal of the Korean Wood Science and Technology
    • /
    • v.42 no.2
    • /
    • pp.183-192
    • /
    • 2014
  • For the structure determination of D-(+)-sucrose, which consists of ${\alpha}$-D-(+)-glucose and ${\beta}$-D-(+)-fructose, it was acetylated with acetic anhydride and triethyl amine, pyridine, zinc chloride, and sodium acetate as catalysts. The acetylated D-(+)-sucrose was acid-hydrolyzed using sulfuric acid and sodium chloride in methanolic solution. The structures of the reaction products were determined by $^1H$-NMR and $^{13}C$-NMR spectra. The yield of the acetylation indicated the high value in zinc chloride as 70% in zinc chloride catalyst. The acid-hydrolyzed product of the acetylated D-(+)-sucrose, 2,3,4,6,1',3',4',6'-octa-O-acetyl-D-(+)-sucrose, gave 2,3,4,6-tetra-O-acetyl-${\beta}$-D-(+)-glucose and it suggests that the acetylated D-(+)-sucrose was rearranged through the formation of oxonium ion by mutarotation in the 2,3,4,6-tetra-O-acetyl-${\alpha}$-D-(+)-glucose moiety and through the ring opening in the 1',3',4',6'-tetra-O-acetyl-${\beta}$-D-(+)-fructose moiety.