Disease relevance of Electrophoresis, Paper

• The index is significantly increased in hypothyroidism and pregnancy, and decreased in hyperthyroidism, correlating well with the TBG capacity measured by reverse-flow paper electrophoresis [1].

High impact information on Electrophoresis, Paper

• The purification of this substance was accomplished by n-butyl chloride extraction of acidified (pH 3.0) uremic sera followed by column chromatography, thin-layer chromatography, and paper electrophoresis [2].
• From its amino acid composition, NH2-terminal residue, mobility in paper electrophoresis, and behavior in high-performance liquid chromatography and from the tryptic pattern of the performic acid-oxidized material, it appears that the inhibitor is identical to the Kunitz and Northrop pancreatic trypsin inhibitor [3].
• The latter could be isolated by extraction with l-butanol and paper electrophoresis in 30% formic acid and was shown to be intact signal peptide by analysis of peptic fragments and automated Edman degradation [4].
• Paper electrophoresis indicated disulfated anhydro[3H]mannitol, presumably sulfated at C3 and C6, as a major component, along with smaller amounts of monosulfated (presumably 3-sulfated) anhydro[3H]mannitol [5].
• Two endogenous ligands for the brain benzodiazepine-binding sites were isolated from bovine brain through gel filtration, paper electrophoresis, and paper chromatography [6].

Biological context of Electrophoresis, Paper

• Mild acid hydrolysis of the glycoprotein fraction afforded sulfated hexosamine fractions which migrated like N-acetylhexosamine mono- and disulfates by paper chromatography and by paper electrophoresis and exhibited 3H/35S which was in accord with the presence of mono- and disulfated compounds [7].
• High-voltage paper electrophoresis (HVPE) analysis demonstrated the production of mannopine in hairy roots and confirmed the successful transfer of Ri T-DNA (root-inducing transferred DNA) of A. rhizogenes into the I. indigotica genome [8].
• Porcine heparin, whale heparin, and a solvolyzed porcine heparin were deaminated, and sulfated oligosaccharides, compounds 3f, 4f, 3s, 4s, 5, 6, 7s, 10, 11f, 11s, and 13 were isolated from the deamination products by Dowex 1 x 2 (Cl- form) column chromatography and high voltage paper electrophoresis and/or gel filtration on Sephadex G-25 [9].

Anatomical context of Electrophoresis, Paper

• Intestinal contents, tissue and/or portal flow were collected and evaluated for resultant purine metabolites by liquid and paper chromatography and paper electrophoresis [10].
• High-voltage paper electrophoresis was used to assay for histamine synthesis in Limulus tissues incubated with radiolabeled histidine; histamine synthesis was detected in the lateral, median, and ventral eyes and optic nerves and in the visual centers in the brain [11].
• Chemical properties of substance P in the spinal cord and dorsal roots of the cat were examined by gel chromatography and paper electrophoresis [12].
• Defatted bovine pineal glands were extracted with acetic acid and further purified by cation-exchange chromatography, gel filtration and paper electrophoresis [13].

Associations of Electrophoresis, Paper with chemical compounds

• The mobilities during paper electrophoresis of the methionine-containing tryptic peptides obtained from the cell-free product were identical to those obtained from growth hormone synthesized and secreted by the GC cells [14].
• Throughout the purification procedures which involved adsorption onto sulfopropyl (SP)-Sephadex, chromatography on Sephadex G-25 and SP-Sephadex, immunoadsorption on neurotensin-antibody Sepharose and high voltage paper electrophoresis, R-NT displayed the chromatographic and electrophoretic properties of neurotensin [15].
• The presence of galactose-labeled O-linked GlcNAc residues was confirmed by high voltage paper electrophoresis [16].
• The factor was finally identified as glutathione disulfide by high voltage paper electrophoresis, paper chromatography, and liquid column chromatography using an amino acid analyzer [17].
• Large fragments were further purified by CM-cellulose chromatography in urea, and small fragments were purified by high voltage paper electrophoresis [18].

Gene context of Electrophoresis, Paper

• Oligosaccharides released from the two SAP-1 samples by hydrazinolysis were fractionated by paper electrophoresis and by Aleuria aurantia lectin-Sepharose and Bio-Gel P-4 (under 400 mesh) column chromatography [19].
• The larger (NIF-1) and smaller (NIF-2) of the polypeptides were resolved by filtration on Bio-Gel P6 and purified to homogeneity by sequential reverse-phase high performance liquid chromatography and paper electrophoresis [20].
• Heterogeneities of the two ovalbumin glycopeptides, (Man)5(GlcNAc)2Asn and (Man)6(GlcNAc)2Asn, were revealed by borate paper electrophoresis of oligosaccharide alcohols obtained from the glycopeptides by endo-beta-N-acetylglucosaminidase H digestion and NaB3H4 reduction [21].
• The maximum T4-binding capacity of urine TBG, determined by reverse flow paper electrophoresis and equilibrium dialysis, was similar to that of serum TBG [22].
• Species-specific tryptic phosphopeptides were resolved from purified H1 histones using high voltage paper electrophoresis [23].

Analytical, diagnostic and therapeutic context of Electrophoresis, Paper

• The resulting peptides were separated using gel filtration combined with either ion exchange chromatography on phosphocellulose in 6 M urea or high voltage paper electrophoresis [24].
• The purified synthetic peptides were found to be homogeneous by paper electrophoresis, isoelectric focusing in polyacrylamide gel, and thin-layer chromatography [25].
• The glutathione adduct was isolated from the kidney extract of the sunlight-irradiated rat using ion-exchangers and high-voltage paper electrophoresis, and determined by fast-atom-bombardment mass spectrometry [26].
• The N-acetyllactosamine-type glycans were obtained by affinity chromatography on concanavalin A and fractionated by high-voltage paper electrophoresis [27].
• The synthetic peptide showed the same physiochemical and chemical properties as natural apamin in the following tests: paper electrophoresis, amino acid analyses after acid and enzymatic hydrolyses, sequence analysis, electrophoreses after tryptic and chymotryptic digestions [28].

References