Displaying publications 1 - 20 of 51 in total

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  1. Yusof AM, Rahman NA, Wood AK
    Biol Trace Elem Res, 1994;43-45:239-49.
    PMID: 7710833
    Trace elements, such as As, Co, Cr, Hg, Sb, and Zn, were determined by neutron activation analysis (NAA), whereas Cd, Cu, and Pb were determined by graphite furnace atomic absorption spectroscopy (GFAAS) in clam, crab, prawn, swamp cerith, and mussel samples after digestion by microwave heating under controlled conditions before eluting the solutions through a column of a chelating resin, Chelex-100. The standard used in the determination of percentage volatile elements retained by microwave digestion and also in the activation process was Lobster Hepatopancreas TORT-1, whereas known mixed standards were prepared from nitrate salts to determine the efficiency of the separation procedure at a controlled pH. Mercury and lead detected in crabs exceeded the maximum permissible level. Some species also showed a high affinity toward certain elements, and their levels of accumulation in the tissues of these species corresponded with the concentration of these elements in sediments, especially at sites in the vicinity of an industrial zone.
    Matched MeSH terms: Chromatography, Ion Exchange
  2. Yap MK, Fung SY, Tan KY, Tan NH
    Acta Trop, 2014 May;133:15-25.
    PMID: 24508616 DOI: 10.1016/j.actatropica.2014.01.014
    The proteome of Naja sumatrana (Equatorial spitting cobra) venom was investigated by shotgun analysis and a combination of ion-exchange chromatography and reverse phase HPLC. Shotgun analysis revealed the presence of 39 proteins in the venom while the chromatographic approach identified 37 venom proteins. The results indicated that, like other Asiatic cobra venoms, N. sumatrana contains large number of three finger toxins and phospholipases A2, which together constitute 92.1% by weight of venom protein. However, only eight of the toxins can be considered as major venom toxins. These include two phospholipases A2, three neurotoxins (two long neurotoxins and a short neurotoxin) and three cardiotoxins. The eight major toxins have relative abundance of 1.6-27.2% venom proteins and together account for 89.8% (by weight) of total venom protein. Other venom proteins identified include Zn-metalloproteinase-disintegrin, Thaicobrin, CRISP, natriuretic peptide, complement depleting factors, cobra venom factors, venom nerve growth factor and cobra serum albumin. The proteome of N. sumatrana venom is similar to proteome of other Asiatic cobra venoms but differs from that of African spitting cobra venom. Our results confirm that the main toxic action of N. sumatrana venom is neurotoxic but the large amount of cardiotoxins and phospholipases A2 are likely to contribute significantly to the overall pathophysiological action of the venom. The differences in toxin distribution between N. sumatrana venom and African spitting cobra venoms suggest possible differences in the pathophysiological actions of N. sumatrana venom and the African spitting cobra venoms, and explain why antivenom raised against Asiatic cobra venom is not effective against African spitting cobra venoms.
    Matched MeSH terms: Chromatography, Ion Exchange
  3. Yap CF, Tan WS, Sieo CC, Tey BT
    Biotechnol Prog, 2013 Mar-Apr;29(2):564-7.
    PMID: 23364925 DOI: 10.1002/btpr.1697
    NP(Δc375) is a truncated version of the nucleocapsid protein of Newcastle disease virus (NDV) which self-assembles into a long helical structure. A packed bed anion exchange chromatography (PB-AEC), SepFastTM Supor Q pre-packed column, was used to purify NP(Δc375) from clarified feedstock. This PB-AEC column adsorbed 76.2% of NP(Δc375) from the clarified feedstock. About 67.5% of the adsorbed NP(Δc375) was successfully eluted from the column by applying 50 mM Tris-HCl elution buffer supplemented with 0.5 M NaCl at pH 7. Thus, a recovery yield of 51.4% with a purity of 76.7% which corresponds to a purification factor of 6.5 was achieved in this PB-AEC operation. Electron microscopic analysis revealed that the helical structure of the NP(Δc375) purified by SepFast(TM) Supor Q pre-packed column was as long as 490 nm and 22-24 nm in diameter. The antigenicity of the purified NP(Δc375) was confirmed by enzyme-linked immunosorbent assay.
    Matched MeSH terms: Chromatography, Ion Exchange/instrumentation; Chromatography, Ion Exchange/methods*
  4. Wahid NB, Latif MT, Suratman S
    Chemosphere, 2013 Jun;91(11):1508-16.
    PMID: 23336924 DOI: 10.1016/j.chemosphere.2012.12.029
    This study was conducted to determine the composition and source apportionment of surfactant in atmospheric aerosols around urban and semi-urban areas in Malaysia based on ionic compositions. Colorimetric analysis was undertaken to determine the concentrations of anionic surfactants as Methylene Blue Active Substances (MBAS) and cationic surfactants as Disulphine Blue Active Substances (DBAS) using a UV spectrophotometer. Ionic compositions were determined using ion chromatography for cations (Na(+), NH4(+), K(+), Mg(2+), Ca(2+)) and anions (F(-), Cl(-), NO3(-), SO4(2-)). Principle component analysis (PCA) combined with multiple linear regression (MLR) were used to identify the source apportionment of MBAS and DBAS. Results indicated that the concentrations of surfactants at both sampling sites were dominated by MBAS rather than DBAS especially in fine mode aerosols during the southwest monsoon. Three main sources of surfactants were identified from PCA-MLR analysis for MBAS in fine mode samples particularly in Kuala Lumpur, dominated by motor vehicles, followed by soil/road dust and sea spray. Besides, for MBAS in coarse mode, biomass burning/sea spray were the dominant source followed by motor vehicles/road dust and building material.
    Matched MeSH terms: Chromatography, Ion Exchange
  5. Thevarajah M, Nadzimah MN, Chew YY
    Clin Biochem, 2009 Mar;42(4-5):430-4.
    PMID: 19026622 DOI: 10.1016/j.clinbiochem.2008.10.015
    Glycated hemoglobin, measured as HbA1c is used as an index of mean glycemia in diabetic patients over the preceding 2-3 months. Various assay methods are used to measure HbA1c and many factors may interfere with its measurement according to assay method used, causing falsely high or low results.
    Matched MeSH terms: Chromatography, Ion Exchange/methods*
  6. Tan NH, Swaminathan S
    Int. J. Biochem., 1992 Jun;24(6):967-73.
    PMID: 1612186
    1. The L-amino acid oxidase of the monocellate cobra (Naja naja kaouthia) venom was purified to electrophoretic homogeneity. The molecular weight of the enzyme was 112,200 as determined by Sephadex G-200 gel filtration chromatography, and 57,400 as determined by SDS-polyacrylamide gel electrophoresis. 2. The enzyme had an isoelectric point of 8.12 and a pH optimum of 8.5. It showed remarkable thermal stability, and, unlike many venom L-amino acid oxidase, was also stable in alkaline medium. The enzyme was partially inactivated by freezing. 3. The enzyme was very active against L-phenylalanine and L-tyrosine, moderately active against L-tryptophan, L-methionine, L-leucine, L-norleucine, L-arginine and L-norvaline. Other L-amino acids were oxidized slowly or not oxidized. 4. Kinetic studies suggest the presence of a side-chain binding site in the enzyme, and that the binding site comprises of at least four hydrophobic subsites.
    Matched MeSH terms: Chromatography, Ion Exchange
  7. Tan NH, Saifuddin MN
    Biochem. Int., 1989 Oct;19(4):937-44.
    PMID: 2619759
    The L-amino acid oxidase (EC 1. 4. 3. 2) from King cobra (Ophiophagus hannah) venom was purified to electrophoretic homogeneity. The molecular weight of the enzyme was determined to be 140000 when examined by gel filtration and 68000 by SDS-polyacrylamide gel electrophoresis. The enzyme had an isoelectric point of 4.5 and an intravenous LD50 of 5 micrograms/g in mice. It is a glycoprotein and contains two moles of FAD per mole of enzyme. The enzyme exhibited unusual thermal stability and unlike most other venom L-amino acid oxidases, it was stable in alkaline solution and was not inactivated by freezing.
    Matched MeSH terms: Chromatography, Ion Exchange
  8. Tan NH, Arunmozhiarasi A
    Biochem. Int., 1989 Apr;18(4):785-92.
    PMID: 2764979
    An acidic, lethal phospholipase Az was purified to electrophoretic homogeneity from the venom of the Malayan cobra (Naja naja sputatrix). The enzyme has an isoelectric point of 5.58, a molecular weight of 12000, and a medium lethal dose (LD50) of 0.86 micrograms/g in mice by intravenous injection. The enzyme also exhibited weak anticoagulant and edema-forming activities. The amino acid composition of the enzyme is similar to those of other cobra venom phospholipases Az.
    Matched MeSH terms: Chromatography, Ion Exchange
  9. Tan NH, Fung SY, Yap YH
    PMID: 21983189 DOI: 10.1016/j.cbpb.2011.09.009
    A thrombin-like enzyme (termed albolabrase) was isolated in purified form from the venom of Cryptelytrops albolabris (white-lipped tree viper) using high performance anion ion exchange and gel filtration chromatography. The molecular mass of albolabrase was 33.7 kDa as determined by SDS-PAGE and 35.8 kDa as determined by Superose gel filtration chromatography. The N-terminal sequence was determined to be VVGGDECNINE which is homologous to many snake venom thrombin-like enzymes. Albolabrase exhibits both arginine ester hydrolase and arginine amidase activities and the enzyme is fastidious towards tripeptide chromogenic anilide substrates. The fibrinogen clotting activity was optimum at 3mg/mL bovine fibrinogen, and showed distinct species differences in the following decreasing order: bovine fibrinogen>dog fibrinogen≈human fibrinogen>goat fibrinogen. The enzyme failed to clot both rabbit and cat fibrinogens. Reversed-phase HPLC analysis on the breakdown products of fibrinogenolytic action of albolabrase indicated that the enzyme belongs to the AB class of snake venom thrombin-like enzyme. In the indirect ELISA, IgG anti-albolabrase reacted extensively with most crotalid venoms, except with Tropidolaemus wagleri and Calloselasma rhodostoma venoms. The double sandwich ELISA, however, showed that anti-albolabrase reacted strongly only with venoms from the Trimeresurus complex, and that the results support the proposed new taxonomy changes concerning the Trimeresurus complex.
    Matched MeSH terms: Chromatography, Ion Exchange
  10. Tan NH
    PMID: 19770070 DOI: 10.1016/j.cbpc.2009.09.002
    A thrombin-like enzyme, purpurase, was purified from the Cryptelytrops purpureomaculatus (mangrove pit viper) venom using high performance ion-exchange and gel filtration chromatography. The purified sample (termed purpurase) yielded a homogeneous band in SDS-polyacrylamide gel electrophoresis with a molecular weight of 35,000. The N-terminal sequence of purpurase was determined to be VVGGDECNINDHRSLVRIF and is homologous to many other venom thrombin-like enzymes. Purpurase exhibits both arginine ester hydrolase and amidase activities. Kinetic studies using tripeptide chromogenic anilide substrates showed that purpurase is not fastidious towards its substrate. The clotting times of fibrinogen by purpurase were concentration dependent, with optimum clotting activity at 3mg fibronogen/mL. The clotting activity by purpurase was in the following decreasing order: cat fibrinogen>human fibrinogen>dog fibrinogen>goat fibrinogen>rabbit fibrinogen. Reversed-phase HPLC analysis of the products of action of purpurase on bovine fibrinogen showed that only fibrinopeptide A was released. Indirect ELISA studies showed that anti-purpurase cross-reacted strongly with venoms of most crotalid venoms, indicating the snake venom thrombin-like enzymes generally possess similar epitopes. In the more specific double-sandwich ELISA, however, anti-purpurase cross-reacted only with venoms of certain species of the Trimeresurus complex, and the results support the recent proposed taxonomy changes concerning the Trimeresurus complex.
    Matched MeSH terms: Chromatography, Ion Exchange
  11. Tan NH, Tan CS
    Toxicon, 1989;27(3):349-57.
    PMID: 2543103
    Trimeresurus wagleri (speckled pit viper) venom exhibited the usual set of enzyme activities occurring in pit viper venoms but the content of alkaline phosphomonoesterase was unusually high, whereas the proportions of protease and arginine ester hydrolase were very low. The venom also exhibited weak thrombin-like activity but did not exhibit hemorrhagic or anticoagulant activity. Analysis of the Sephadex G-200 gel filtration fractions of the venom indicated that the lethal fraction was a low mol.wt protein, and that fractions exhibiting phosphodiesterase, phosphomonoesterase, arginine ester hydrolase, thrombin-like enzyme, L-amino acid oxidase and phospholipase A activities were not lethal. Two lethal toxins, designated as wagleri toxins 1 and 2, were isolated from the venom using Sephadex G-50 gel filtration chromatography followed by SP-Sephadex C-25 ion exchange chromatography. The mol.wts of the two toxins were 8900 by gel filtration. The LD50 (i.v.) values in mice for wagleri toxins 1 and 2 are 0.17 microgram/g and 0.19 microgram/g, respectively.
    Matched MeSH terms: Chromatography, Ion Exchange
  12. Tan NH, Tan CS
    Toxicon, 1987;25(11):1249-53.
    PMID: 3433296
    The enzymatic activities of four samples of Malayan cobra venom were investigated. There was significant variation in the contents of L-amino acid oxidase, alkaline phosphomonoesterase, acetylcholinesterase, phospholipase A, 5'-nucleotidase and hyaluronidase. The phosphodiesterase content was, however, constant. Storage of the lyophilized venom powder at 25 degrees C for 1 month did not affect the enzymatic activities. The venom enzymatic activities were generally also stable at 4 degrees C in 0.85% saline solution. After incubation at 37 degrees C for 39 days in 0.85% saline solution, the venom still retained considerable amounts of enzymatic activities. SP-Sephadex C-25 ion-exchange chromatography of the venom showed that the phospholipase A, L-amino acid oxidase, 5'-nucleotidase, phosphodiesterase and alkaline phosphomonoesterase exist in multiple forms.
    Matched MeSH terms: Chromatography, Ion Exchange
  13. Tan NH, Poh CH, Tan CS
    Toxicon, 1989;27(9):1065-70.
    PMID: 2799837
    Bungarus candidus venom exhibited high hyaluronidase, acetylcholinesterase and phospholipase A activities; low proteinase, 5'-nucleotidase, alkaline phosphomonoesterase and phosphodiesterase activities and moderately high L-amino acid oxidase activity. SP-Sephadex C-50 ion exchange chromatographic fractionation of the venom and Sephadex G-50 chromatography of the major lethal venom fractions indicate that the venom contains at least two highly lethal, basic phospholipases A with LD50 (i.v.) values of 0.02 micrograms/g (F6A) and 0.18 micrograms/g (F4A), respectively; as well as two polypeptide toxins with LD50 (i.v.) values of 0.17 micrograms/g and 0.83 micrograms/g, respectively. The major lethal toxin is the basic lethal phospholipase A, F6A, which accounts for approximately 13% of the venom protein and has a mol. wt of 21,000.
    Matched MeSH terms: Chromatography, Ion Exchange
  14. Tan NH, Tan CS
    Toxicon, 1989;27(6):697-702.
    PMID: 2749766
    Sumatran pit viper (Trimeresurus sumatranus sumatranus) venom was fractionated by DEAE-Sephacel ion exchange chromatography into seven fractions. Fractions 4, 5 and 6 were lethal to mice and exhibited strong hemorrhagic activity, as well as some enzymatic activities. Fraction 6 also exhibited potent anticoagulant and thrombin-like activities. Analysis of the biological and enzymatic properties of the three lethal fractions suggests that the major lethal component of fractions 4 and 5 may be the hemorrhagic principle, and that the lethality of fraction 6 may be due to the hemorrhagic principle and/or the anticoagulant principle.
    Matched MeSH terms: Chromatography, Ion Exchange
  15. Song CP, Ooi CW, Tey BT, Lu CX, Liu BL, Chang YK
    Int J Biol Macromol, 2020 Dec 01;164:4455-4465.
    PMID: 32937154 DOI: 10.1016/j.ijbiomac.2020.09.051
    A stirred fluidized bed (SFB) ion exchange chromatography was successfully applied in the direct recovery of recombinant enhanced green fluorescent protein (EGFP) from the unclarified Escherichia coli homogenate. Optimal conditions for both adsorption and elution processes were determined from the packed-bed adsorption systems conducted at a small scale using the clarified cell homogenate. The maximal adsorption capacity and dissociation constant for EGFP-adsorbent complex were found to be 6.3 mg/mL and 1.3 × 10-3 mg/mL, respectively. In an optimal elution of EGFP with 0.2 M of NaCl solution (pH 9) and at 200 cm/h, the recovery percent of the EGFP was approximately 93%. The performances of SFB chromatography for direct recovery of EGFP was also evaluated under different loading volumes (50-200 mL) of crude cell homogenate. The single-step purification of EGFP by SFB recorded in a high yield (95-98%) and a satisfactory purification factor (~3 folds) of EGFP from the cell homogenate at 200 rpm of rotating speed.
    Matched MeSH terms: Chromatography, Ion Exchange/instrumentation; Chromatography, Ion Exchange/methods*
  16. Soda W, Noble AD, Suzuki S, Simmons R, Sindhusen LA, Bhuthorndharaj S
    J. Environ. Qual., 2006 Oct 27;35(6):2293-301.
    PMID: 17071900
    Acid waste bentonite is a byproduct from vegetable oil bleaching that is acidic (pH < 3.0) and hydrophobic. These materials are currently disposed of in landfills and could potentially have a negative impact on the effective function of microbes that are intolerant of acidic conditions. A study was undertaken using three different sources of acid waste bentonites, namely soybean oil bentonite (SB), palm oil bentonite (PB), and rice bran oil bentonite (RB). These materials were co-composted with rice husk, rice husk ash, and chicken litter to eliminate their acid reactivity and hydrophobic nature. The organic carbon (OC) content, pH, exchangeable cations, and cation exchange capacity (CEC) of the acid-activated bentonites increased significantly after the co-composting phase. In addition, the hydrophobic nature of these materials as measured using the water drop penetration time (WDPT) decreased from >10 800 s to 16 to 80 s after composting. Furthermore, these composted materials showed positive impacts on soil physical attributes including specific surface area, bulk density, and available water content for crop growth. Highly significant increases in maize biomass (Zea mays L.) production over two consecutive cropping cycles was observed in treatments receiving co-composted bentonite. The study clearly demonstrates the potential for converting an environmentally hazardous material into a high-quality soil conditioner using readily available agricultural byproducts. It is envisaged that the application of these composted acid waste bentonites to degraded soils will increase productivity and on-farm income, thus contributing toward food security and poverty alleviation.
    Matched MeSH terms: Chromatography, Ion Exchange
  17. Show PL, Ooi CW, Song CP, Chai WS, Lin GT, Liu BL, et al.
    Food Chem, 2021 May 01;343:128543.
    PMID: 33187742 DOI: 10.1016/j.foodchem.2020.128543
    Lysozyme from crude chicken egg white (CEW) feedstock was successfully purified using a stirred fluidized bed adsorption system ion exchange chromatography where STREAMLINE SP and SP-XL high density adsorbents were selected as the adsorption carrier. The thermodynamic and kinetic studies were carried out to understand the characteristics of lysozyme adsorption by adsorbents under various conditions, including adsorption pH, temperature, lysozyme concentration and salt concentrations. Results showed that SP and SP-XL adsorbents achieved optimum lysozyme adsorption at pH 9 with capacity of ~139.77 and ~251.26 mg/mL, respectively. The optimal conditions obtained from batch studies were directly employed to operate in SFBA process. For SP-XL adsorbent, the recovery yield and purification factor of lysozyme were 93.78% and ~40 folds, respectively. For SP adsorbent, lysozyme can be eluted ~100% with purification factor of ~26 folds. These two adsorbents are highly suitable for use in direct recovery of lysozyme from crude CEW.
    Matched MeSH terms: Chromatography, Ion Exchange/methods*
  18. Rahman RN, Baharum SN, Basri M, Salleh AB
    Anal Biochem, 2005 Jun 15;341(2):267-74.
    PMID: 15907872
    An organic solvent-tolerant S5 lipase was purified by affinity chromatography and anion exchange chromatography. The molecular mass of the lipase was estimated to be 60 kDa with 387 purification fold. The optimal temperature and pH were 45 degrees C and 9.0, respectively. The purified lipase was stable at 45 degrees C and pH 6-9. It exhibited the highest stability in the presence of various organic solvents such as n-dodecane, 1-pentanol, and toluene. Ca2+ and Mg2+ stimulated lipase activity, whereas EDTA had no effect on its activity. The S5 lipase exhibited the highest activity in the presence of palm oil as a natural oil and triolein as a synthetic triglyceride. It showed random positional specificity on the thin-layer chromatography.
    Matched MeSH terms: Chromatography, Ion Exchange
  19. Ong KK, Khor HT, Tan DT
    Anal Biochem, 1991 Aug 01;196(2):211-4.
    PMID: 1776669
    A rapid, easy, and sensitive method is described in this paper for the assay of 3-hydroxy-3-methylglutaryl CoA (HMG CoA) reductase, a key enzyme in cholesterol biosynthesis. [14C]HMG CoA was used as the substrate and the product formed, i.e., [14C]mevalonate, was allowed to be converted to its lactone form (mevalonolactone) in the presence of HCl. The reaction mixture was applied to a column containing an anionic exchanger. The column was made up of QAE-Sephadex (A25, formate form) packed to a height of 4 cm in Pasteur pipets. Under these conditions, mevalonolactone was not retained by the column and was eluted with ammonium formate solution while HMG CoA, being negatively charged, was retained by the gel and eluted by HCl above 0.05 M. Determination of the amount of radioactivity in mevalonolactone was then used to quantitate the activity of HMG CoA reductase. This assay has been successfully used for determining the activity of this enzyme in a microsomal fraction prepared from the liver of the rat.
    Matched MeSH terms: Chromatography, Ion Exchange/methods*
  20. Nget Hong Tan, Chon Seng Tan
    Toxicon, 1988;26(11):989-96.
    PMID: 3245058
    The toxic and biological activities of four samples of Trimeresurus purpureomaculatus venom were examined. The lethality, protein composition and biological activities of the four venom samples were similar. Three of the venom samples had LD50 (i.v.) values of 0.9 micrograms/g while the fourth had a lower LD50 (i.v.) of 0.45 micrograms/g. All four venom samples exhibited hemorrhagic, edema-inducing, anticoagulant and thrombin-like activities as well as the usual enzymes found in crotalid venoms. DEAE-Sephacel ion exchange chromatographic fractionation of the venom yielded 10 protein fractions. Only two fractions (fractions A and F) were lethal to mice; the major lethal fraction being fraction F. This fraction had an LD50 (i.v.) of 0.2 micrograms/g and exhibited hemorrhagic, edema-inducing and thrombin-like activity. It also exhibited phospholipase A, arginine ester hydrolase, arginine amidase, protease, 5'-nucleotidase, acetylcholinesterase and alkaline phosphomonoesterase activities. The lethal potency of fraction F is potentiated by fraction G, which exhibited anticoagulant activity as well as hemorrhagic, edema-inducing and enzymatic activities. Fractions F plus G account for almost 100% of the lethal potency of the venom.
    Matched MeSH terms: Chromatography, Ion Exchange
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