Disease relevance of Sephadex G 25

• Escherichia coli P16 infant mouse active heat-stable enterotoxin may be fractionated into two distinct active moieties by ion-exchange chromatography, Sephadex G-25 chromatography, and isoelectric focusing [1].
• The sera of 4 patients with bullous pemphigoid, of 5 patients with drug reactions and of 13 patients with atopic eczema were examined for the occurrence of low molecular weight eosinophil chemotactic factor (ECF) by fractionation on a Sephadex G 25 column [2].
• Urinary proteins from patients with iron deficiency anemia and acquired aplastic anemia were fractionated by chromatography on QAE-Sephadex A-50 and Sephadex G-25 [3].
• 3. Ultrafiltrates ( less than 10 000 daltons) of serum were chromatographed on Sephadex G-25 and the elution profile obtained from patients with fulminant hepatic failure was both qualitatively and quantitatively different from that of normal controls [4].
• ADH immunoreactive extracts of six lung tumours and nine metastases (all oat cell) showed the same pattern on elution from a Sephadex G-25 column [5].

High impact information on Sephadex G 25

• Gel filtration of the extracts of the pancreas and stomach on Sephadex G-25 yielded two immunoreactive peaks, one corresponding in each case to the somatostatin tetradecapeptide [6].
• To determine whether taxol remained bound to tubulin subunits, we subjected depolymerized taxol-treated microtubule protein to Sephadex G-25 chromatography, and the fractions were assayed for taxol content by reverse-phase HPLC [7].
• Because insulin-stimulated CKII activity was maintained after chromatography of cell extracts on Sephadex G-25, it is unlikely that the effect is mediated by a low-molecular-weight activator of the kinase [8].
• The difference in MAP-2 kinase activity in extract supernatants from control and insulin-treated cells is also preserved after rapid chromatography on Sephadex G-25 [9].
• "Transfer factor" was prepared by Sephadex G-25 chromatography of lymph node cell lysates from guinea pigs immunized with ovalbumin or bovine gamma globulin [10].

Chemical compound and disease context of Sephadex G 25

• To elucidate the chemical structures of penicillin polymers that may elicit an allergic reaction, a 25% aqueous solution of penicillin G potassium was kept standing in the dark at room temperature for 14 days and was then separated by gel filtration chromatography on Sephadex G-25 [11].
• In this study, we provide evidence that the ability of the purified low-pH inactivated (citrate buffer, pH 3.0) and gel-filtered (Sephadex G-25) HSZP virions to adsorb host cells was not significantly affected [12].
• Acidocin 8912, a bacteriocin produced by Lactobacillus acidophilus TK8912, was purified by ammonium sulfate fractionation and successive chromatographies on CM-cellulose, Sephadex G-50, Sephadex G-25, and reversed-phase HPLC on Aquapore RP-300 [13].
• Acidic ethanol precipitation, gel-filtration chromatography (Sephadex G-25) and capillary isotachophoresis were performed on serum and tumor tissue samples from eight patients with stage III and IV laryngeal cancers [14].
• By SDS-PAGE or gel filtration on Sephadex G-25, lipopolysaccharide (LPS) isolated from Vibrio cholerae 569B (Inaba) can be separated into two distinct fractions, one corresponding to smooth LPS and the other to rough LPS [15].

Biological context of Sephadex G 25

• After hydrolysis of the alpha chain with trypsin, chymotrypsin, and thermolysin, radioactive peptides were isolated by gel filtration on Sephadex G-25 and reversed-phase high performance liquid chromatography [16].
• The isolation procedure included ultrafiltration, gel chromatography on Sephadex G-25, and preparative paper chromatography, Structural determination involved sugar and methylation analyses [17].
• The soluble factor(s) that increased Fc-mediated phagocytosis passed through both 6000- to 8000-dalton and 2000-dalton cutoff dialysis membranes and eluted from a Sephadex G-25 Fine column over a m.w. range of 200 to 1000 daltons, with a peak activity at 450 daltons [18].
• The ratio of bound to free T4 (B/F) is first determined for two total-T4 concentrations using a Sephadex G-25 competitive-binding technique [19].
• To analyze the active site of parotid protein, the parotid subunit (PS) was digested by trypsin and then fractionated on a Sephadex G-25 column [20].

Anatomical context of Sephadex G 25

• These activated lectins were purified on a Sephadex G-25 column and showed the binding affinity to an affinity column, glucosylated Sepharose, and to the human erythrocyte ghost membrane [21].
• Previous studies from other laboratories, using rabbit reticulocyte lysate filtered through Sephadex G-25 or G-50, have demonstrated that glucose 6-phosphate is required to maintain active rates of translation, but its mechanism of action is currently unsettled [22].
• A transfer factor-like activity was prepared by Sephadex G-25 chromatography of immune guinea pig leukocyte lysates [23].
• The phospholipid mediator 1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphorylcholine (AGEPC) increases human polymorphonuclear leukocyte (PMN) adherence to Sephadex G-25 in manner directly proportional to the concentration of AGEPC from 2 to 650 nM [24].
• Human serum, or serum proteins excluded by Sephadex G-25, irreversibly inhibited the ability of mouse pancreatic islet cells to accumulate Rb+ [25].

Associations of Sephadex G 25 with other chemical compounds

• However, filtration of the same factors on Sephadex G-25 in 0.1 M acetic acid revealed one predominant fibroblast-activating activity for each cell source of an apparent m.w. of 500 to 1000 [26].
• After treatment with 0.05 M NaOH, 1 M NaBH4 at 45 degrees C for 24 h, two major sialic acid-containing oligosaccharides were observed on Sephadex G-25, corresponding to penta- and hexasaccharides [27].
• Most of the epinephrine effect on the rat heart supernatant kinase is retained at 0 degrees if cAMP is removed by Sephadex G-25 chromatography, although this procedure completely reverses the epinephrine effect in the guinea pig heart [28].
• Separation of pronase glycopeptides by gel filtration on Sephadex G-25 revealed that 96% of the carbohydrate is present in the highest molecular weight fraction which contains 60% of the threonine of mycodextranase but only 3.5% of the aromatic acids judged by its absorbance at 280 nm [29].
• [3H]Triamcinolone acetonide-labeled cytosolic GR was transformed, using Sephadex G-25 filtration, to yield the RNA-containing 6 S GR [30].

Gene context of Sephadex G 25

• Sephadex G-25 gel filtration of the ME extracts showed one peak for AVP and two peaks for CRF [31].
• Binding of fluoresceinated IL-2 to different cell types was assessed by flow cytometry analysis, on a FACS 440 calibrated using fluoresceinated Sephadex G-25 beads [32].
• These results suggest that AVP in NIAMDD-Rat HE-RP-1 is polymerized or aggregated on the Sephadex G-25 column, especially when eluted in 0.2M acetic acid [33].
• What was measured in these sera showed identity to synthetic SRIF on serial dilutions, Sephadex G-25 chromatography, and thin-layer chromatography, and it was shown to be immunoreactive by an antibody-Sepharose affinity system [34].
• 3. Two of the major pathological oligosaccharides, GP5 and GP6, were purified by chromatography on charcoal/Celite and Sephadex G-25 [35].

Analytical, diagnostic and therapeutic context of Sephadex G 25

• The same Sephadex G-25 gel filtration fraction previously shown to contain the "uremic" inhibitor was tested in both the isolated toad bladder and rat bioassay systems [36].
• The assay procedure consisted of intraperitoneal injection into mice of aliquots of plasma, previously chromatographed on Sephadex G-25 [37].
• The pooled peak of PGF-A activity from Sephadex G-25 filtration and CM52 chromatography eluted as a single peak at 0.024 M NH4HCO3 on DE52 [38].
• This substance also co-migrated with synthetic AVP on both Sephadex G-25 and reverse-phase thin layer chromatography (RPTLC) [39].
• They were separated by paper chromatography and were characterized by Sephadex G-25 column chromatography, by affinity column chromatography on concanavalin A-Sepharose, and by successive digestion with alpha-mannosidase and beta-mannosidase [40].

References