PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25617389-0 2015 Resolving Transferrin Isoforms via Agarose Gel Electrophoresis. Sepharose 35-42 transferrin Homo sapiens 10-21 25617389-8 2015 CONCLUSION: Agarose electrophoresis with the MOPS-histidine buffer increases the resolution of transferrin isoforms. Sepharose 12-19 transferrin Homo sapiens 95-106 11570502-6 2001 As an example, we demonstrate that more than 95% of the human transferrin receptor bound to a transferrin-sepharose ligand affinity column can be eluted with full binding activity at KSCN concentrations between 232 and 414 nM, whereas elution with urea is not suitable to purify fully functional protein. Sepharose 106-115 transferrin Homo sapiens 62-73 16755932-1 2006 Human transferrin receptor (TfR) was isolated from homogenates of placental tissues by affinity chromatography on transferrin-Sepharose, and then used to screen human scFv against it from a fully-synthesized phage scFv library. Sepharose 126-135 transferrin Homo sapiens 6-17 12113980-6 2002 Especially in case of the Sepharose Q FF, Mono Q 5/5 HR and Hitrap Q XL columns the vanadium-transferrin binding was degraded during elution on the column. Sepharose 26-35 transferrin Homo sapiens 93-104 11570502-6 2001 As an example, we demonstrate that more than 95% of the human transferrin receptor bound to a transferrin-sepharose ligand affinity column can be eluted with full binding activity at KSCN concentrations between 232 and 414 nM, whereas elution with urea is not suitable to purify fully functional protein. Sepharose 106-115 transferrin Homo sapiens 94-105 8732060-1 1995 The human placenta transferrin receptor was purified in the form of transferrin-transferrin receptor complex (Tf-TfR), and a monospecific polyclonal antibody against TfR was developed by a Tf-coupled Sepharose 4B affinity chromatography to remove the anti-Tf components in the antiserum. Sepharose 200-212 transferrin Homo sapiens 19-30 9916061-11 1999 Subjecting the cell surface extract to affinity chromatography on an agarose-transferrin column revealed that it contained a protein having an estimated molecular mass of 37 kDa and possessing transferrin-binding activity. Sepharose 69-76 transferrin Homo sapiens 77-88 9916061-11 1999 Subjecting the cell surface extract to affinity chromatography on an agarose-transferrin column revealed that it contained a protein having an estimated molecular mass of 37 kDa and possessing transferrin-binding activity. Sepharose 69-76 transferrin Homo sapiens 193-204 9238529-2 1997 We have developed a procedure for isolating TFR from human placental tissues by affinity chromatography on transferrin-Sepharose. Sepharose 119-128 transferrin Homo sapiens 107-118 7558284-6 1995 All of the strains displayed a transferrin binding phenotype, and affinity isolation of receptor proteins with transferrin-conjugated Sepharose recovered Tbp1 and/or Tbp2 from 11 of 14 strains, including 2 of the nontypeable biotype IV strains. Sepharose 134-143 transferrin Homo sapiens 111-122 8535287-3 1995 We demonstrated, using a sepharose-bead-Tf complex, the rapid recycling of unoccupied internal transferrin receptors was correlated with ligand binding to surface receptors. Sepharose 25-34 transferrin Homo sapiens 95-106 8069555-5 1993 Determination of the interaction between avidin-pLys460-]bio-transferrin] and DNA was carried out by nitro cellulose filter binding and agarose gel retardation assays. Sepharose 136-143 transferrin Homo sapiens 61-72 7496925-2 1994 The beta-2 transferrin was detected by agarose gel electrophoresis of the fluid on Beckman Paragon equipment, followed by pressure transfer to a nitrocellulose membrane and then incubation with enzyme-labeled antitransferrin antibody and substrate. Sepharose 39-46 transferrin Homo sapiens 11-22 1482396-2 1992 Transferrin receptors were isolated from the solubilized membranes by affinity chromatography on diferric transferrin-coupled Sepharose 4B. Sepharose 126-138 transferrin Homo sapiens 0-11 1482396-2 1992 Transferrin receptors were isolated from the solubilized membranes by affinity chromatography on diferric transferrin-coupled Sepharose 4B. Sepharose 126-138 transferrin Homo sapiens 106-117 1791429-1 1991 Each of two affinity isolation methods, the first based on biotinylated porcine transferrin plus streptavidin-agarose, and the second on Sepharose-coupled porcine transferrin, followed by SDS-PAGE, allowed the isolation and identification of two potential porcine-transferrin-binding polypeptides (approximately 64 kDa and 99 kDa) from total membranes of Actinobacillus pleuropneumoniae grown under iron-restricted conditions. Sepharose 137-146 transferrin Homo sapiens 163-174 1791429-1 1991 Each of two affinity isolation methods, the first based on biotinylated porcine transferrin plus streptavidin-agarose, and the second on Sepharose-coupled porcine transferrin, followed by SDS-PAGE, allowed the isolation and identification of two potential porcine-transferrin-binding polypeptides (approximately 64 kDa and 99 kDa) from total membranes of Actinobacillus pleuropneumoniae grown under iron-restricted conditions. Sepharose 137-146 transferrin Homo sapiens 163-174 1791429-3 1991 The 64 kDa polypeptide was the more easily removed from Sepharose-coupled porcine transferrin and only the 99 kDa polypeptide appeared to be an outer-membrane protein. Sepharose 56-65 transferrin Homo sapiens 82-93 2806210-1 1989 Several genetic variants and also isoforms of transferrin differing in carbohydrate structure can be separated by polyacrylamide or agarose gel isoelectric focusing. Sepharose 132-139 transferrin Homo sapiens 46-57 1906465-2 1991 The nascent transferrin receptor containing core-glycosylated asparagine-linked oligosaccharides does not possess complete intersubunit disulfide bonds, sediments predominantly as a monomer in sucrose density gradients, and shows reduced binding to transferrin-agarose. Sepharose 261-268 transferrin Homo sapiens 12-23 2137090-9 1990 Transferrin-binding ability of MA-PG was studied by affinity column chromatography, using CNBr-activated sepharose bound to transferrin. Sepharose 105-114 transferrin Homo sapiens 0-11 2137090-9 1990 Transferrin-binding ability of MA-PG was studied by affinity column chromatography, using CNBr-activated sepharose bound to transferrin. Sepharose 105-114 transferrin Homo sapiens 124-135 2571374-1 1989 OBJECTIVE: To assess the value of serum carbohydrate deficient transferrin as detected by isoelectric focusing on agarose as an indicator of alcohol abuse. Sepharose 114-121 transferrin Homo sapiens 63-74 2126013-4 1990 Internalization of 125I-biotin-S-S-transferrin (125I-BSST) was quantitated by adsorption to avidin-Sepharose after treatment of cells with GSH. Sepharose 99-108 transferrin Homo sapiens 35-46 6086661-4 1984 Transferrin receptors from uninduced and differentiating cells were partially purified by affinity chromatography on transferrin-Sepharose and shown to be disulfide-bridged homodimers of a polypeptide with an apparent molecular weight of approximately 90,000. Sepharose 129-138 transferrin Homo sapiens 0-11 2543820-1 1989 An affinity procedure with purified, biotinylated human transferrin and streptavidin-agarose was used to identify the transferrin-binding proteins in strains of Haemophilus influenzae. Sepharose 85-92 transferrin Homo sapiens 118-129 2543489-6 1989 The transferrin- and lactoferrin-binding proteins were identified after affinity isolation using biotinylated human transferrin or lactoferrin and streptavidin-agarose. Sepharose 160-167 transferrin Homo sapiens 4-15 3047122-8 1988 About 30% of human transferrin receptors made in insect cells do not form intermolecular disulfide bonds, but are recognized by the anti-transferrin receptor antibody, B3/25, and bind specifically to a human transferrin-Sepharose column. Sepharose 220-229 transferrin Homo sapiens 19-30 3047122-8 1988 About 30% of human transferrin receptors made in insect cells do not form intermolecular disulfide bonds, but are recognized by the anti-transferrin receptor antibody, B3/25, and bind specifically to a human transferrin-Sepharose column. Sepharose 220-229 transferrin Homo sapiens 137-148 3047122-8 1988 About 30% of human transferrin receptors made in insect cells do not form intermolecular disulfide bonds, but are recognized by the anti-transferrin receptor antibody, B3/25, and bind specifically to a human transferrin-Sepharose column. Sepharose 220-229 transferrin Homo sapiens 137-148 3281751-7 1988 In soft agarose, both HCT 116 and HCT 116a subpopulations showed a stringent requirement for transferrin. Sepharose 8-15 transferrin Homo sapiens 93-104 2428547-0 1986 Microheterogeneity of human transferrin as revealed by agarose gel electrophoresis with an iron-specific stain. Sepharose 55-62 transferrin Homo sapiens 28-39 6467619-1 1984 Isoelectric focusing in agarose gel has been used for separation of different molecular forms of transferrin (Tf) in sera and plasma from alcoholics and controls. Sepharose 24-31 transferrin Homo sapiens 97-108 6467619-1 1984 Isoelectric focusing in agarose gel has been used for separation of different molecular forms of transferrin (Tf) in sera and plasma from alcoholics and controls. Sepharose 24-31 transferrin Homo sapiens 110-112 2722854-4 1989 The 85-kDa, as well as the 93-kDa, receptors bound to a monoclonal antibody raised against the transferrin receptor or to transferrin-Sepharose. Sepharose 134-143 transferrin Homo sapiens 95-106 2920013-2 1989 By affinity chromatography on a concanavalin A-Sepharose column in well-defined conditions, human serotransferrin isolated from healthy donors was resolved into three carbohydrate molecular variants: Tf-I (less than 1%), Tf-II (17 +/- 2%) and Tf-III (82 +/- 3%) containing two triantennary glycans, one triantennary and one biantennary glycans and two biantennary glycans respectively. Sepharose 47-56 transferrin Homo sapiens 98-113 2437241-0 1987 [Detection of beta 2-transferrin with agarose gel electrophoresis, immunofixation and silver staining in cerebrospinal fluid, secretions and other body fluids]. Sepharose 38-45 transferrin Homo sapiens 21-32 2437241-3 1987 The high sensitivity and specificity of the test depend on immunofixation of the electrophoretically separated transferrin in the agarose gel, and on the visualization of the immune complex by staining with alkaline silver nitrate solution. Sepharose 130-137 transferrin Homo sapiens 111-122 6573952-6 1983 This protein was identified as the transferrin receptor by affinity absorption of extracts of 125I-surface protein-labeled cells to transferrin-Sepharose beads. Sepharose 144-153 transferrin Homo sapiens 35-46 6309862-12 1983 Extracting ATR-gold complexes with Triton X after a 30-min chase at 22 degrees C and purifying them on Sepharose-transferrin indicated that the internalized complexes remained bound to the transferrin receptor during their intracellular processing. Sepharose 103-112 transferrin Homo sapiens 113-124 6309862-12 1983 Extracting ATR-gold complexes with Triton X after a 30-min chase at 22 degrees C and purifying them on Sepharose-transferrin indicated that the internalized complexes remained bound to the transferrin receptor during their intracellular processing. Sepharose 103-112 transferrin Homo sapiens 189-200 6573952-6 1983 This protein was identified as the transferrin receptor by affinity absorption of extracts of 125I-surface protein-labeled cells to transferrin-Sepharose beads. Sepharose 144-153 transferrin Homo sapiens 132-143 6268632-3 1981 Gel filtration on acrylamide agarose (AcA-22) at 23 degrees C in the absence of transferrin indicates the transferrin receptor has a Stokes radius of 4.6 nm. Sepharose 29-36 transferrin Homo sapiens 106-117 6828455-4 1983 The polyacrylamide P-6 bead has a greater density of surface groups than the Sepharose bead, and this correlates to the greater density of transferrin receptors on erythroblasts. Sepharose 77-86 transferrin Homo sapiens 139-150 6296151-2 1983 The first method involves affinity chromatography of the transferrin receptor with a transferrin-linked Sepharose 4B resin. Sepharose 104-116 transferrin Homo sapiens 85-96 6790617-3 1981 A similar protein is precipitated by transferrin-agarose, but not by agarose alone. Sepharose 49-56 transferrin Homo sapiens 37-48 7030111-3 1981 In this investigation serum transferrin from healthy controls and alcoholic patients was purified by affinity chromatography on antitransferrin Sepharose 4B. Sepharose 144-156 transferrin Homo sapiens 28-39 6790617-4 1981 Peptide mapping by limited proteolysis shows that the proteins precipitated by OKT-9 antibodies and transferrin-agarose are homologous. Sepharose 112-119 transferrin Homo sapiens 100-111 1189627-0 1975 Transferrin variants designated by their relative mobilities in high-voltage agarose gel electrophoresis. Sepharose 77-84 transferrin Homo sapiens 0-11 851436-0 1977 Iron transport from Sepharose-bound transferrin. Sepharose 20-29 transferrin Homo sapiens 36-47 6270664-2 1981 Antisera developed in a goat against purified human placental transferrin binding protein was purified by fractional sodium sulfate precipitation and adsorption against Sepharose-bound transferrin to remove trace anti-transferrin activity. Sepharose 169-178 transferrin Homo sapiens 62-73 6270664-2 1981 Antisera developed in a goat against purified human placental transferrin binding protein was purified by fractional sodium sulfate precipitation and adsorption against Sepharose-bound transferrin to remove trace anti-transferrin activity. Sepharose 169-178 transferrin Homo sapiens 185-196 6270664-2 1981 Antisera developed in a goat against purified human placental transferrin binding protein was purified by fractional sodium sulfate precipitation and adsorption against Sepharose-bound transferrin to remove trace anti-transferrin activity. Sepharose 169-178 transferrin Homo sapiens 185-196 6306643-3 1981 Gel filtration on acrylamide agarose (AcA-22) at 21 degrees C in the absence of transferrin indicates that the transferrin-binding protein has a Stokes" radius of 4.6 nm. Sepharose 29-36 transferrin Homo sapiens 111-122 1014940-0 1976 [Preparation of pure albumin and transferrin from rabbit serum using con A-sepharose]. Sepharose 75-84 transferrin Homo sapiens 33-44 1189627-1 1975 A unified nomenclature for the designation of transferrin variants, based on their relative mobilities in a standardized high-voltage agarose gel electrophoresis, is proposed. Sepharose 134-141 transferrin Homo sapiens 46-57 6038133-0 1967 Determination of transferrin by Laurell electrophoresis in antibody containing agarose gel. Sepharose 79-86 transferrin Homo sapiens 17-28 33454336-5 2021 Native agarose gel analysis showed changes in mobility of human transferrin upon Fe3+ binding. Sepharose 7-14 transferrin Homo sapiens 64-75