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Journal articles on the topic 'Gel filtration chromatography'

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Published: 4 June 2021

Last updated: 20 February 2023

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1

Werner, Milton H., G. Marius Clore, Angela M. Gronenborn, Akiko Kondoh, and Robert J. Fisher. "Refolding proteins by gel filtration chromatography." FEBS Letters 345, no. 2-3 (May 30, 1994): 125–30. http://dx.doi.org/10.1016/0014-5793(94)00401-3.

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2

Barnes, Ana Isabel, Cristina Ortiz, María Gabriela Paraje, Luis Eduardo Balanzino, and Inès Albesa. "Purification and characterization of a cytotoxin fromEnterobacter cloacae." Canadian Journal of Microbiology 43, no. 8 (August 1, 1997): 729–33. http://dx.doi.org/10.1139/m97-105.

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Leukotoxic activity was assayed in clinical isolates of Enterobacter cloacae. Two strains were selected out of 38 by their greater hemolytic activity in blood agar plates. Leukotoxin was purified by salt precipitation, dialysis, chromatography by gel filtration, and high pressure liquid chromatography (HPLC). Human leukocytes, when incubated with purified E. cloacae toxin, showed high percentages of death and lysis, with time and dose dependence. The chromatographic profile of gel filtration presented three protein peaks and toxic activity was detected in the second peak. After HPLC, leukotoxin coeluted with the hemolytic activity and both activities were detected only after 2-mercaptoethanol treatment. Coomassie-stained sodium dodecyl sulfate – polyarylamide gels showed a single band. This band was estimated to represent a protein of 13 300 Da on the basis of both sodium dodecyl sulfate – polyacrylamide gel electrophoresis and gel filtration chromatography.Key words: Enterobacter clocae, leukotoxin, molecular mass, cytotoxin, leukocytes.

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3

Hunt, Eric A., and Sapna K. Deo. "Board-Game Gel Filtration and Affinity Chromatography." Journal of Chemical Education 86, no. 1 (January 2009): 19. http://dx.doi.org/10.1021/ed086p19.

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4

Wooten, Arthur L., M. Lynn Prewitt, Terry Sellers, and David C. Teller. "Gel filtration chromatography of resole phenolic resins." Journal of Chromatography A 445 (January 1988): 371–76. http://dx.doi.org/10.1016/s0021-9673(01)84549-0.

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5

Girona, V., J. Estelrich, M. Pujol, and J. Bolòs. "Ampicillin polymers: identification by gel-filtration chromatography." International Journal of Pharmaceutics 41, no. 3 (February 1988): 241–44. http://dx.doi.org/10.1016/0378-5173(88)90200-1.

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6

Kumar Shaha, Ranajit, Nitai Roy, and Talukdar G. "Characterization and Sensitivity Test of the Allergenic Pollen Proteins from Litchi Chimensis Plant." Journal of Tropical Resources and Sustainable Science (JTRSS) 1, no. 1 (August 15, 2021): 25–35. http://dx.doi.org/10.47253/jtrss.v1i1.667.

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Pollen of Litchi chinensis (Litchi) is a major aeroallergen of Bangladesh. Pollen of this fruits plant was collected from full bloomed flower growing in different places of Rajshahi in Bangladesh. Pollen protein was extracted and partial purified by means of long-term PBS extraction, salting out, dialysis, gel filtrations and DEAE-Cellulose chromatography and the protein was designated as LFPP (Litchi flowers pollen protein). Gel filtration of the purified pollen protein gives two main peaks. The major peak gives four bands on SDS-PAGE. The enzyme (pectate lyase) proteins after gel filtration again re-purified by Ion exchange chromatography, a single band in the protein profile of LFPP, (M.W. 28kDa) was the major allergenic component of Litchi chinensis (Litchi) flower pollen. The homogeneity and the molecular weight of the protein were estimated by SDS-PAGE, and Gel filtration was 28kDa. The allergenic protein was identified by skin prick tests and showed the pectate lyase (Pel) activity. Skin-prick tests also revealed highest degree of sensitivity to the Nawabgang sample giving positive response in 80% of the patients. Skin reactivity ranged between 1+ and 3+.

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7

Russo, Salvatore F., and Angie Radcliffe. "Separations utilizing gel filtration and ion-exchange chromatography." Journal of Chemical Education 68, no. 2 (February 1991): 168. http://dx.doi.org/10.1021/ed068p168.

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8

González, Ana, and Jaime Gómez-Márquez. "Purification of bacteriophage DNA by gel filtration chromatography." Gene Analysis Techniques 7, no. 1 (February 1990): 2–4. http://dx.doi.org/10.1016/0735-0651(90)90037-g.

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9

Whisenant, E. C., B. K. A. Rasheed, and Y. M. Bhatnagar. "Plasmid purification using high-performance gel filtration chromatography." Nucleic Acids Research 16, no. 11 (1988): 5202. http://dx.doi.org/10.1093/nar/16.11.5202.

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10

Nitoda, Teruhiko, Hirokazu Usuki, and Hiroshi Kanzaki. "A Potent Insect Chitinase Inhibitor of Fungal Origin." Zeitschrift für Naturforschung C 58, no. 11-12 (December 1, 2003): 891–94. http://dx.doi.org/10.1515/znc-2003-11-1226.

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Abstract A water-soluble polysaccharide was isolated from the culture filtrate of a fungal strain, Sphaeropsis sp. TNPT116-Cz, as a novel insect chitinase inhibitor. It was purified to chromatographic homogeneity by ethanol precipitation, anion-exchange and gel filtration chromatography. Its molecular weight was estimated to be 16 kDa by gel filtration HPLC. Monosaccharide analysis showed that it contained glucose, galactose, N-acetylglucosamine and a deoxysugar. This polysaccharide showed potent and specific inhibitory activity against Spodoptera litura chitinase with an IC50 value of 28 nᴍ.

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11

Alaubydi, Mouruj A., Susan Ahmad, and Muayad Sabri. "Preparation of antibodies type IgY against Salmonella typhi lipopolysaccharide in chicken eggs." Journal of Biotechnology Research Center 6, no. 2 (June 1, 2012): 15–22. http://dx.doi.org/10.24126/jobrc.2012.6.2.214.

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ipopolysaccharide was extracted from local isolate Sallmonella typhi (previously isolated and characterized) by hot EDTA method, and the extract was partially purified by gel filtration chromatography on sepharose Cl-6B gel. The results showed that the percentage of the carbohydrates amount in the partially purified LPS extract was 43.7%, while the percentage of binding proteins in the same extract was 0.7% with no nucleic acids was found. The molecular weight for the LPS was measured by the gel filtration chromatography method using Sepharose Cl-6B gel and was equivalent to 263000 Dalton. The LD¬50 of LPS was determined by injection of chicken embryos type Ice Brown in the charioallantoic membrane, and was 14.66 µg/Kg. In order to obtain anti S. typhi IgY antibodies, chickens were immunized with the partially purified S. typhi subcutaneously. The IgY antibodies were extracted from eggs yolk by water dilution method and the extract was partially purified by ammonium sulphate precipitation at ratio 60% saturation, and gel filtration chromatography on sepharose Cl-6B gel. The results showed that the protein amount was equivalent to 23.5 mg/ml; specific activity was 0.268, and an overall yield of 70%. The molecular weight for the IgY antibodies was measured by the gel filtration chromatography method using Sepharose Cl-6B gel and was found to be 178000 dalton. The concentration of anti S.typhi LPS IgY antibodies in chicken eggs were investigated by ELISA and was found to be 6.3 mg/ml, and there is a significant differences (P<0.01).

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12

Rahman, H., A. W. Skillen, S. M. Channon, M. K. Ward, and D. N. Kerr. "Methods for studying the binding of aluminum by serum protein." Clinical Chemistry 31, no. 12 (December 1, 1985): 1969–73. http://dx.doi.org/10.1093/clinchem/31.12.1969.

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Abstract We describe methods for studying the binding of Al by protein in serum: ultrafiltration, gel filtration, and immuno-affinity chromatography. For ultrafiltration we used an Amicon YM10 cellophane membrane with a nominal cutoff of 10 000 Da to separate ultrafiltrable and non-ultrafiltrable Al. For gel filtration we used Sephacryl S-300, and for immuno-affinity chromatography we used anti-transferrin coupled to CNBr-activated Sepharose to identify the Al-binding protein. For 30 normal subjects 54% of the total Al in serum was non-ultrafiltrable; for 30 patients with chronic renal failure being treated by hemodialysis 67% was non-ultrafiltrable. In both groups transferrin was identified as the major Al-binding protein in the serum. Results of gel-filtration studies should be interpreted with caution: some gel media adsorb "free" Al, which can be subsequently taken up by transferrin or desferrioxamine passing through the column. We find affinity chromatography to be a specific and reliable method, suitable for use in quantitative studies.

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13

Martosuyono, Pujoyuwono, Asri Pratitis, Alexander Prasetya, and Elisabeth Kartika Prabawati. "DESALINATION OF CHITOOLOGOSACCAHARIDES USING GEL FILTRATION AND ULTRAFILTRATION." Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology 9, no. 3 (December 3, 2014): 127. http://dx.doi.org/10.15578/squalen.v9i3.110.

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Chitooligosaccharide (COS) , which is a derivative product from chitosan, has recently been used as a functional food because it has antimicrobial, antifungal, and antitumor properties. The salt content in chitooligosaccharide is one of the main problems in application as functional food or pharmaceutical medicine. The aim of this study was to remove salt from COS with two desalting techniques and determine the variation of COSs in the product. The desalting technique used were dialysis with 10kD Molecular Weight Cut Off (MWCO) and gel filtration chromatography HiPrep 26/10 desalting with G-25 Superfine Sephadex as stationary phase in the column. In order to detect the presence of COS, Thin Layer Chromatography (TLC) method was used, followed by Matrix-Assisted Laser Desorption-Ionization Time-of-Flight Mass Spectrometry (MALDI–TOF–MS) to detect low concentration of COS. Qualitative and quantitative analysis of salt presence were identified using silver nitrate and Volhard method respectively. Ash content was measured using gravimetric method. Results showed those dialysis and gel filtration chromatographies were successfully remove the most of the salt from COS with efficiency of desalting up to 100%. However, the best desalting technique was gel filtration chromatography HiPrep 26/10 which has more complete COS with various degrees of polymerization present in the result.

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14

TAMAKI, Masako, Mitsuko UKAI, and Seiichi HOMMA. "Gel Filtration Chromatography of Browned Compounds in Heated Onion." NIPPON SHOKUHIN KAGAKU KOGAKU KAISHI 43, no. 12 (1996): 1293–98. http://dx.doi.org/10.3136/nskkk.43.1293.

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15

SNOW, S. D., and J. R. BROOKS. "Fractionation of Rice Glutelin Polypeptides using Gel Filtration Chromatography." Journal of Food Science 54, no. 3 (May 1989): 730–33. http://dx.doi.org/10.1111/j.1365-2621.1989.tb04691.x.

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16

Yamamoto, Shuichi, Masaki Nomura, and Yuji sano. "Predicting the performance of gel-filtration chromatography of proteins." Journal of Chromatography A 512 (July 1990): 77–87. http://dx.doi.org/10.1016/s0021-9673(01)89474-7.

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17

Kim, Hyungwon, and In Ho Kim. "Refolding of fusion ferritin by gel filtration chromatography (GFC)." Biotechnology and Bioprocess Engineering 10, no. 6 (December 2005): 500–504. http://dx.doi.org/10.1007/bf02932284.

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18

Wilson, N., V. Yakoleff, and R. Keeler. "Big ANF: large-molecular-weight ANF in plasma. I. Gel filtration and affinity chromatography studies." American Journal of Physiology-Endocrinology and Metabolism 261, no. 4 (October 1, 1991): E516—E524. http://dx.doi.org/10.1152/ajpendo.1991.261.4.e516.

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A large molecular form of immunoreactive atrial natriuretic factor (irANF) was demonstrated in plasma of rabbit and rat on the basis of gel filtration experiments. This big ANF was not retained by octadecylsilane cartridges and cross-reacted with four anti-ANF antisera of different specificities. Gel filtration in acid, but not in 8 M urea, resulted in material with elution characteristics of irANF. Affinity chromatography and gel electrophoresis of big ANF suggested that the material was similar to albumin. However, high concentrations of big ANF were found in analbuminemic rats, with characteristics similar to those seen in rabbit and normal rats (affinity and gel chromatography and gel electrophoresis). We thus conclude that big ANF represents a bound form of ANF in circulation and that the carrier is similar to but not identical with albumin.

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19

Yukalo, Volodymyr, Kateryna Datsyshyn, and Liudmyla Storozh. "OBTAINING OF Β-LACTOGLOBULIN BY GEL FILTRATION OF COW MILK WHEY." EUREKA: Life Sciences 2 (March 31, 2019): 33–39. http://dx.doi.org/10.21303/2504-5695.2019.00859.

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Milk whey proteins carry out a number of important biological functions and also they are precursors of many biologically active peptides (antihypertensive peptides, antagonists of opioid receptors, regulators of intestinal motility, immunomodulatory, anti-microbial and anti-cancer peptides, appetite regulators and so on.). An important stage in natural bioactive peptides obtaining from milk whey proteins is the isolation of homogeneous proteins-precursors. Considering the significant difference in the molecular masses of whey proteins, a promising method for their selection is gel filtration. The purpose of the research was the fractionation of bioactive peptides precursors from milk whey using gel filtration on Sephadex G-150. The whey was obtained from fresh skimmed milk after isoelectric precipitation of casein. Gel filtration was carried out on the columns from a liquid chromatography kit by the “Reanal” company. The fractional composition and the degree of homogeneity of milk whey proteins were determined by disc-electrophoresis in the plates of a polyacrylamide gel. A repeated gel filtration of fractions from the chromatographic peaks, separated into sections, was performed to increase the fractionation efficiency. While choosing a dextran gel for gel filtration of precursors of biologically active peptides from milk whey proteins, we have taken into account the range of their molecular weights (from 10000 to 150000 Da), the ability to form supramolecular structures (β-LG), as well as the previously obtained results of gel filtration. As a result, it was shown that repeated gel filtration of milk whey on Sephadex G-150 allows efficiently fractionate the proteins-precursors of bioactive peptides. The range of peptides and proteins molecular weights that can be fractionated on this Sephadex is from 5000 to 300 000 Da. The usage of repeated gel filtration on Sephadex G-150 with the chromatogram separation into sectors allows to effectively fractionate proteins-precursors of bioactive peptides from milk whey. In particular, homogeneous β-lactoglobulin (degree of homogeneity > 95 %) and partially purified α-lactalbumin, as well as a group of immunoglobulins and a proteose-peptone fraction were obtained.

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20

Hassani, Hayfa H., and Rawa'a J. Toma. "Influence of various levels of L-asparaginase II purification on the cytotoxicity, DNA level, and apoptosis in Hep-2 cells." Journal of Biotechnology Research Center 4, no. 2 (June 1, 2010): 46–52. http://dx.doi.org/10.24126/jobrc.2010.4.2.121.

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The genetic effects of several concentrations of L–Asparaginase II (ASNase II), produced by Proteus vulgaris strain Pv.U92, at various levels of purification (ultrasonication, precipitation, ion-exchange chromatography and gel filtration chromatography) on cancer cells line of Hep–2 were studied. This bacterial enzyme with concentration 4 U/ml at gel filtration level was revealed a putative cytotoxicity against cancer cells in comparison with other concentrations and steps of purification were used in this work. Moreover, 4 U/ml of ASNase II at gel purification level has a distinguished role on arrest cancer cells division of Hep–2; it was reduced the content of DNA at each phase of cancer cell cycle particularly at G2/M phase, the level of DNA was 3%. On the other hand, the partial purified enzyme, L–ASNase II, was induced apoptosis by both levels of purification ion–exchange and gel filtration, the apoptotic fractionation was 0.86 and 0.7 respectively .

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21

Ooi, L. SM, T. B. Ng, Yunqi Geng, and V. EC Ooi. "Lectins from bulbs of the Chinese daffodil Narcissus tazetta (family Amaryllidaceae)." Biochemistry and Cell Biology 78, no. 4 (April 3, 2000): 463–68. http://dx.doi.org/10.1139/o00-052.

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The isolation of three lectins with similar N-terminal amino acid sequences from the bulbs of the Chinese daffodil Narcissus tazetta was achieved. The isolation protocol involved ion exchange chromatography on DEAE-cellulose, affinity chromatography on mannose-agarose, and fast protein liquid chromatography-gel filtration on Superose 12. The lectins were all adsorbed on mannose-agarose and demonstrated a single band with a molecular weight of 13 kDa in SDS-polyacrylamide gel electrophoresis and a single 26 kDa peak in gel filtration, indicating that they were mannose-binding, dimeric proteins. The lectins differed in hemagglutinating activity, with the magnitude of the activity correlating with the ionic strength of the buffer required to elute the lectin from the DEAE-cellulose column. The bulb lectin did not exert potent cytotoxicity against cancer cell lines or fetal bovine lung cells but inhibited syncytium formation in, and reinstated viability of, fetal bovine lung cells infected with bovine immunodeficiency virus.Key words: lectins, daffodil bulbs, chromatography.

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22

Mercer, E., T. E. Cawston, M. de Silva, and B. L. Hazleman. "Purification of a metalloproteinase inhibitor from human rheumatoid synovial fluid." Biochemical Journal 231, no. 3 (November 1, 1985): 505–10. http://dx.doi.org/10.1042/bj2310505.

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A metalloproteinase inhibitor present in human rheumatoid synovial fluid was purified by a combination of heparin-Sepharose chromatography, concanavalin A-Sepharose chromatography, ion-exchange chromatography and gel filtration. The Mr of the purified inhibitor was 28000 by SDS/polyacrylamide-gel electrophoresis and 30000 by gel filtration. The inhibitor blocked the activity of the metalloproteinases collagenase, gelatinase and proteoglycanase, but not thermolysin or bacterial collagenase. The serine proteinase trypsin was not inhibited. The inhibitory activity was lost after treatment with trypsin (0.5 micrograms/ml) at 37 degrees C for 30 min, 4-aminophenylmercuric acetate (1 mM) at 37 degrees C for 3 h, after incubation for 30 min at 90 degrees C and by reduction and alkylation. These properties suggest that the inhibitor closely resembles the tissue inhibitor of metalloproteinases (‘TIMP’) recently purified from connective-tissue culture medium.

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23

Jonáková, Věra, Brigita Vidimská, Jana Urbanová, and Manfred Pavlík. "Isolation and partial characterization of boar proacrosin." Collection of Czechoslovak Chemical Communications 55, no. 3 (1990): 846–53. http://dx.doi.org/10.1135/cccc19900846.

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Boar proacrosin was purified to apparent homogeneity by a three-step procedure: gel filtration on Sephadex G-50 medium, ion-exchange chromatography on CM-Cellulose 32, and reversed-phase high-performance liquid chromatography on a C4 column. The relative molecular mass (Mr) of the proacrosin estimated by gel filtration was about 70 000, whereas the results of an electrophoretic experiment on SDS-polyacrylamide gel with copolymerized casein under non-reducing conditions indicated an Mr of 55 000-60 000. The proacrosin reproducibly migrated on the gel as a double band. When purified, it remained stable at pH 8.0 for 30 min. The amino-acid composition of the homogeneous proacrosin was determined, the N-terminal amino-acid sequence being Arg-Asp-X-Ala-Thr-X-X-Gly-Pro-X-Gly-.

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24

Pen, J., J. Van Beeumen, and J. J. Beintema. "Structural comparison of two esterases from Drosophila mojavensis isolated by immunoaffinity chromatography." Biochemical Journal 238, no. 3 (September 15, 1986): 691–99. http://dx.doi.org/10.1042/bj2380691.

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Antibodies raised against esterase-4 and esterase-5 from Drosophila mojavensis were coupled to Protein A-Sepharose CL-4B to prepare high-efficiency immunomatrices used for their purification. Final purification was achieved by anion-exchange h.p.l.c., in the case of esterase-5 followed by gel-filtration h.p.l.c. The resultant esterase preparations were homogeneous, as judged by gel-filtration h.p.l.c., SDS/polyacrylamide-gel electrophoresis and non-denaturing gel electrophoresis. Esterase-4 and esterase-5 are the products of a duplicated gene. They are differently localized in the insect's body and expressed in different periods during development. Although both enzymes exhibit little immunological cross-reactivity, their amino acid compositions show few significant differences and their N-terminal sequences are largely identical, which clearly show their common origin.

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25

Blahovec, Ján, Michal Bartík, and Evžen Kasafírek. "Isolation and partial characterization of bovine liver aminopeptidase B." Collection of Czechoslovak Chemical Communications 50, no. 5 (1985): 1249–57. http://dx.doi.org/10.1135/cccc19851249.

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Aminopeptidase B, specifically hydrolyzing the L-lysine and L-arginine derivatives of p-nitroaniline and β-naphthylamine, was isolated from bovine liver. A multistep purification procedure involving fractionation with ammonium sulfate, gel filtration on Sephadex, ion exchange chromatography on Ecteola-cellulose, and adsorption chromatography on hydroxylapatite, afforded an enzyme whose activity was approximately 240 times higher than the activity of the original material. The molecular weight of the enzyme determined by gel filtration on Sephadex G-200 was approximately 55 000. The Michaelis constant with respect to L-lysyl-p-nitroanilide was 1.2 . 10-3 mol/l.

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26

Filho, Edivaldo Ximenes Ferreira. "Purification and characterization of a β-glucosidase from solid-state cultures ofHumicola griseavar.thermoidea." Canadian Journal of Microbiology 42, no. 1 (January 1, 1996): 1–5. http://dx.doi.org/10.1139/m96-001.

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The thermophilic fungus Humicola grisea var. thermoidea produced β-glucosidase activity when grown in a solid-state culture on wheat bran as carbon source. A β-glucosidase was purified to apparent homogeneity by ultrafiltration, gel filtration chromatography on Sephacryl S-100, and ion-exchange chromatography on S-Sepharose, as judged by sodium dodecyl sulfate – polyacrylamide gel electrophoresis (SDS–PAGE) on a 12.5% (w/v) slab gel. The enzyme had a molecular mass of 82 and 156 kDa, as estimated by SDS–PAGE and gel filtration on a high performance liquid chromatographic column, respectively, suggesting that the native enzyme may consist of two identical subunits. The purified enzyme was thermostable at 60 °C for 1 h with a half-life of 15 min at 65 °C, and displayed optimum activity at 60 °C and a pH range of 4.0–4.5. The Kmand Vmaxvalues for p-nitrophenyl β-D-glucopyranoside were determined to be 0.316 mM and 0.459 IU∙mL−1, respectively. D-Glucose, D-gluconic acid lactone, Hg2+, Cu2+, and Mn2+inhibited β-glucosidase activity. The enzyme activity was competitively inhibited by D-glucose (Ki = 0.6 mM). The purified enzyme was very active against cellobiose and p-nitrophenyl β-D-glucopyranoside.Key words: Humicola, β-glucosidase, purification, characterization.

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27

Gao, P., J. Li, Z. Li, J. Hao, and L. Zan. "Establishment and application of milk fingerprint by gel filtration chromatography." Journal of Dairy Science 99, no. 12 (December 2016): 9493–501. http://dx.doi.org/10.3168/jds.2015-10655.

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28

Sauterer, Roger A., and Jody Jones. "A Rapid, Simple & Inexpensive Experiment in Gel Filtration Chromatography." American Biology Teacher 62, no. 8 (October 1, 2000): 602–7. http://dx.doi.org/10.2307/4450986.

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29

KITAMURA, Takashi, Seiji ITO, Yoshio KATO, Keiko SASAMOTO, and Mitsuyo OKAZAKI. "Analysis of serum lipoproteins by high performance gel filtration chromatography." Bunseki kagaku 45, no. 1 (1996): 103–6. http://dx.doi.org/10.2116/bunsekikagaku.45.103.

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30

Sauterer, Roger A., and Jody Jones. "A Rapid, Simple & Inexpensive Experiment in Gel Filtration Chromatography." American Biology Teacher 62, no. 8 (October 2000): 602–7. http://dx.doi.org/10.1662/0002-7685(2000)062[0602:arsiei]2.0.co;2.

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31

Yamamoto, Susumu. "Determination of haptoglobin types by high-performance gel filtration chromatography." Japanese Journal of Oral Biology 34, no. 4 (1992): 364–73. http://dx.doi.org/10.2330/joralbiosci1965.34.364.

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32

SUDO, Jun-ichi, Taiji HAYASHI, Jun TERUI, Toshihiko SUZUE, Momoko SOYAMA, and Midori TATEYAMA. "Urinary albumin determination by gel-filtration high-performance liquid chromatography." Journal of Toxicological Sciences 17, no. 3 (1992): 107–18. http://dx.doi.org/10.2131/jts.17.107.

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33

Rothman, Ronald J., and Leonard Warren. "Analysis of IgG glycopeptides by alkaline borate gel filtration chromatography." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 955, no. 2 (July 1988): 143–53. http://dx.doi.org/10.1016/0167-4838(88)90188-4.

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34

Grummer, Ric R., Connie A. Meacham, Walter L. Hurley, and Carl L. Davis. "Apolipoprotein composition of bovine lipoproteins isolated by gel filtration chromatography." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 88, no. 4 (January 1987): 1163–74. http://dx.doi.org/10.1016/0305-0491(87)90020-4.

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35

YAMAMOTO, SHUICHI, MASAKI NOMURA, and YUJI SANO. "Scaling up of medium-performance gel filtration chromatography of proteins." Journal of Chemical Engineering of Japan 19, no. 3 (1986): 227–31. http://dx.doi.org/10.1252/jcej.19.227.

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36

McKenna, Sean A., Insil Kim, Elisabetta Viani Puglisi, Darrin A. Lindhout, Colin Echeverría Aitken, R. Andrew Marshall, and Joseph D. Puglisi. "Purification and characterization of transcribed RNAs using gel filtration chromatography." Nature Protocols 2, no. 12 (December 2007): 3270–77. http://dx.doi.org/10.1038/nprot.2007.480.

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37

Chu, Yongbao, Baoyu Gao, Qinyan Yue, Yan Wang, and Shuguang Wang. "Characterization and separation of Al13 species using gel-filtration chromatography." Science in China Series B: Chemistry 49, no. 4 (August 2006): 326–31. http://dx.doi.org/10.1007/s11426-006-0326-4.

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38

Bergeron, Chantal, Andrew Marston, Etienne Hakizamungu, and Kurt Hostettmann. "ANTIFUNGAL CONSTITUENTS OF CHENOPODIUM PROCERUM (CHENOPODIACEAE) HOCHST EX MOQ." HortScience 29, no. 4 (April 1994): 254a—254. http://dx.doi.org/10.21273/hortsci.29.4.254a.

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Dried ground aerial parts were extracted successively with dichloromethane and methanol at room temperature. Antifungal activity was determined by a TLC bioassay using Cladosporium cucumerinum. Four compounds were isolated from a dichloromethane extract by different chromatographic techniques (silicagel CC, Sephadex LH-20 gel filtration, and low-pressure LC on Diol): the isoflavones irilin A and irilin B, the flavonone dihydrowogonin, and sesquiterpene pygmol. The latter three were antifungal. The minimal amount that inhibited the fungal growth of C. cucumerinum was 5 μ for these compounds. Four flavonol glycosides were obtained from the non-fungicidal extract by Sephadex LH-20 gel filtration and centrifugal partition chromatography. The structures of the compounds were elucidated by spectroscopic methods (UV, 1H NMR, 13CNMR, MS).

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39

Dieuleveux, V., D. Van Der Pyl, J. Chataud, and M. Gueguen. "Purification and Characterization of Anti-Listeria Compounds Produced by Geotrichum candidum." Applied and Environmental Microbiology 64, no. 2 (February 1, 1998): 800–803. http://dx.doi.org/10.1128/aem.64.2.800-803.1998.

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ABSTRACT Geotrichum candidum can produce and excrete compounds that inhibit Listeria monocytogenes. These were purified by ultrafiltration, centrifugal partition chromatography, thin-layer chromatography, gel filtration, and high-pressure liquid chromatography, and analyzed by liquid chromatography-mass spectrometry, infrared spectrometry, nuclear magnetic resonance spectrometry, and optical rotation. Two inhibitors were identified:d-3-phenyllactic acid and d-3-indollactic acid.

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40

Winzor, D. J. "The development of chromatography for the characterization of protein interactions: a personal perspective." Biochemical Society Transactions 31, no. 5 (October 1, 2003): 1010–14. http://dx.doi.org/10.1042/bst0311010.

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This article reviews the progress of a personal endeavour to develop chromatography as a quantitative procedure for the determination of reaction stoichiometries and equilibrium constants governing protein interactions. As well as affording insight into an aspect of chromatography with which many protein chemists are unfamiliar, it shows the way in which minor adaptations of conventional chromatographic practices have rendered the technique one of the most powerful methods available for the characterization of interactions. That pathway towards quantification is followed from the introduction of frontal gel filtration for the study of protein self-association to the characterization of ligand binding by the biosensor variant of quantitative affinity chromatography.

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41

Quinn, C. P., C. C. Shone, P. C. B. Turnbull, and J. Melling. "Purification of anthrax-toxin components by high-performance anion-exchange, gel-filtration and hydrophobic-interaction chromatography." Biochemical Journal 252, no. 3 (June 15, 1988): 753–58. http://dx.doi.org/10.1042/bj2520753.

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A procedure has been developed for purification of the tripartite anthrax-toxin components. This involves sequential high-performance anion-exchange, gel-filtration and hydrophobic-interaction chromatography. From an initial culture volume of 15 litres, typical yields of 8 mg of protective antigen, 13 mg of lethal factor and 7 mg of oedema factor are produced to higher degrees of purity than have previously been achieved by conventional chromatographic techniques.

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42

Qian, RL, K. Chin, JK Kim, HM Chin, J. Cone, and WD Hankins. "Purification of murine erythropoietin produced in serum-free cultures of erythroleukemia cells." Blood 68, no. 1 (July 1, 1986): 258–62. http://dx.doi.org/10.1182/blood.v68.1.258.258.

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Abstract We previously documented that several erythroleukemia cell lines released factors that stimulated erythropoiesis in vivo and in vitro. A simple five-step scheme has been devised that allows purification of this erythropoietic activity to apparent homogeneity. The methods employed included lectin affinity chromatography (wheat germ agglutinin), gel filtration (ultro gel ACA44), ion exchange, hydroxylapatite, and high performance liquid chromatography. Following polyacrylamide gel electrophoresis, biologic activity was recovered in an area corresponding to a molecular weight of 35,000 daltons. Silver staining of a polyacrylamide gel after electrophoresis of our most purified preparation revealed a single band at 35,000 daltons.

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43

Qian, RL, K. Chin, JK Kim, HM Chin, J. Cone, and WD Hankins. "Purification of murine erythropoietin produced in serum-free cultures of erythroleukemia cells." Blood 68, no. 1 (July 1, 1986): 258–62. http://dx.doi.org/10.1182/blood.v68.1.258.bloodjournal681258.

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We previously documented that several erythroleukemia cell lines released factors that stimulated erythropoiesis in vivo and in vitro. A simple five-step scheme has been devised that allows purification of this erythropoietic activity to apparent homogeneity. The methods employed included lectin affinity chromatography (wheat germ agglutinin), gel filtration (ultro gel ACA44), ion exchange, hydroxylapatite, and high performance liquid chromatography. Following polyacrylamide gel electrophoresis, biologic activity was recovered in an area corresponding to a molecular weight of 35,000 daltons. Silver staining of a polyacrylamide gel after electrophoresis of our most purified preparation revealed a single band at 35,000 daltons.

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44

Barberis, Lucila Isabel, Alberto Jorge Eraso, Maria Cristina Pàjaro, and Inès Albesa. "Molecular weight determination and partial characterization of Klebsiella pneumoniae hemolysins." Canadian Journal of Microbiology 32, no. 11 (November 1, 1986): 884–88. http://dx.doi.org/10.1139/m86-161.

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Two thiol-activated Klebsiella pneumoniae hemolysins were purified from growth media by means of salt precipitation, gel filtration, ion-exchange chromatography, and polyacrylamide gel electrophoresis. The hemolysins peaks coincided with the protein and glycoprotein peaks as determined by chromatography and electrophoresis, The molecular weights, estimated by gel filtration, were 8400 and 19 000; by sodium dodecyl sulphate–polyacrylamide gel electrophoresis, the values were calculated as 15 500 and 27 000. The electrophoretic bands were best detected by the periodic acid–Schiff method. Reduction of the disulfide linkages did not cause the originally larger molecule to break into 8400 and 19 000 hemolysins. However, trypsin treatment cleaved the 19 000 hemolysin into an active moiety, with an electrophoretic migration similar to the 8400 hemolysin. A naturally occurring proteolytic activity was investigated using pepstatin and antipain. When the trypsin inhibitor was added to the system, the hemolytic activity was detected only in the 19 000 hemolysin and the smaller hemolysin was absent.

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45

Svensson, B. E., K. Domeij, S. Lindvall, and G. Rydell. "Peroxidase and peroxidase-oxidase activities of isolated human myeloperoxidases." Biochemical Journal 242, no. 3 (March 15, 1987): 673–80. http://dx.doi.org/10.1042/bj2420673.

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Isolated neutrophils from healthy donors were used for the isolation of four highly purified forms of myeloperoxidase as determined by spectral (A430/A280 ratio 0.80-0.87) and enzyme-activity measurements. Although the myeloperoxidases exhibited different elution profiles on cation-exchange chromatography, gel filtration indicated similar relative molecular masses. When these forms were assayed for peroxidase and peroxidase-oxidase activities with several substrates, they all exhibited virtually the same specific activities. These results suggest that possible functional differences between the enzymes may be related to differences in their sites of action rather than to differences in enzyme activity. Myeloperoxidase from a patient with chronic myeloid leukaemia also revealed a similar heterogeneity on cation-exchange chromatography. However, this myeloperoxidase contained in addition one form with a lower and one form with a higher relative molecular mass, as indicated by gel-filtration chromatography.

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46

Edwards, Judson V., and Eivind B. Lillehoj. "Isolation and Liquid Chromatographic Determination of the Cyclic Peptide Mycotoxin Cyclosporin A from Rice." Journal of AOAC INTERNATIONAL 70, no. 1 (January 1, 1987): 126–29. http://dx.doi.org/10.1093/jaoac/70.1.126.

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Abstract A simple method for determination and quantitation of a cyclic peptide mycotoxin, cyclosporin A, in rice is presented. Rice inoculated with Trichoderma polysporum (Link ex Pers.) was extracted with methylene chloride after 4 weeks of incubation. Cyclosporin A was isolated from extracts by using open bed gel filtration column chromatography (LH-20, acetonitrile) and monitored with thin layer chromatography and reverse phase liquid chromatography coelution with a standard. Preliminary thin layer chromatographic methods were developed. Cyclosporin A was detected by iodine and after partial acid hydrolysis by ninhydrin and UV light. A liquid chromatographic method was developed that used a reverse phase disposable cartridge cleanup and isocratic chromatography with a reverse phase octadecylsilica column and a UV detector set at 212 nm. Recovery of cyclosporin A from spiked rice samples (mg/g range) was 85%.

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47

Savic, Ivan M., Goran S. Nikolic, Stanko A. Zerajic, and Ivana M. Savic. "Gel filtration chromatography analysis and modeling the process of pullulan depolymerization." Journal of Polymer Engineering 32, no. 4-5 (August 1, 2012): 225–33. http://dx.doi.org/10.1515/polyeng-2011-0104.

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Abstract Different fractions of pullulan oligosaccharide can be applied in the synthesis of pharmaceutical active compounds. Thus, the object of this study was to model the depolymerization process of pullulan polysaccharide with the change of pH, temperature and depolymerization time. The samples were analyzed by gel filtration chromatography (GFC). The chromatography separation of polymer fractions was achieved by using a Zorbax PSM-300 HP-SEC column (250×6.2 mm, 5 μm) at a temperature of 25°C. The flow rate of the mobile phase (redistilled water) was 1 cm3 min-1. The fractions were recorded by a refractive index detector. The obtained data were converted by thin plate spline interpolation function into matrixes. By the mathematical processing matrixes, the models of molar mass distribution in the function of pH, temperature and depolymerization time were obtained. The intervals of depolymerization parameters can be defined for obtaining the desirable pullulan oligomers, which have the efficient applications in macromolecule technology.

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48

Peerce, B. E., M. Cedilote, S. Seifert, R. Levine, C. Kiesling, and R. D. Clarke. "Reconstitution of intestinal Na(+)-phosphate cotransporter." American Journal of Physiology-Gastrointestinal and Liver Physiology 264, no. 4 (April 1, 1993): G609—G616. http://dx.doi.org/10.1152/ajpgi.1993.264.4.g609.

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The rabbit intestinal brush-border membrane Na(+)-phosphate cotransporter was purified from sodium dodecyl sulfate (SDS)-brush-border membrane vesicles (BBMV) protein (SDS-treated Ca(2+)-precipitated BBMV) by a three-column chromatography protocol. The purification included a preparative scale chromatofocusing chromatography column over the pH range from 7.4 to 4 after solubilization in 3-[(3-cholamidopropyl)-diamethylammonia]-1-propanesulfonate (CHAPS), a chromatofocusing column over the pH range from 5.6 to 4 after solubilization in n-octyl glucoside, and gel filtration chromatography on a Sephacryl S-200 column. Verification of Na(+)-phosphate cotransporter purification involved substrate affinities, substrate stoichiometry, and inhibitor sensitivity after proteoliposome reconstitution and SDS-polyacrylamide gel electrophoresis (PAGE). After gel filtration Na(+)-dependent phosphate uptake was 3,300-fold enriched compared with the cell homogenate. A single 130-kDa polypeptide was visualized by SDS-PAGE under reducing conditions using silver stain. The coenrichment of this 130-kDa polypeptide and proteoliposome reconstituted Na(+)-dependent phosphate uptake suggest that the intestinal brush-border membrane Na(+)-phosphate cotransporter has been purified and proteoliposome reconstituted.

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49

TAKAHASHI, Sadao, Toshitaka TAMAI, Hirotada TAKAI, Shinta HAYASHI, Hajime MAEDA, Hiroyuki SAGE, Tsuguhiko INAKA, and Susumu MIYABO. "Lipoproteins Separation on Superose 6 Gel-Filtration Column Using Fast Protein Liquid Chromatography System." Journal of Japan Atherosclerosis Society 15, no. 5 (1987): 1179–83. http://dx.doi.org/10.5551/jat1973.15.5_1179.

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50

Changui, Cherkaoui, William E. E. Stone, and L�on Vielvoye. "Characterisation of a partially neutralised aluminium solution using gel-filtration chromatography." Analyst 115, no. 9 (1990): 1177. http://dx.doi.org/10.1039/an9901501177.

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