PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12523650-7 2002 A fusion protein of glutathione-S-transferase and human progastrin(1-80) was expressed in Escherichia coli, collected on glutathione-agarose beads, and cleaved with enterokinase. Sepharose 133-140 glutathione S-transferase kappa 1 Homo sapiens 20-45 12811499-2 2003 GST isoenzyme(s) were first separated on the basis of their affinity to glutathione sepharose 4B affinity column. Sepharose 84-96 glutathione S-transferase kappa 1 Homo sapiens 0-3 15177873-3 2004 The GST-hTFF3 fusion protein was expressed in Escherichia coli, and hTFF3 was purified with Glutathione Sepharose 4B affinity chromatography, yielding about 3-4 mg of pure hTFF3 in one liter of culture broth. Sepharose 104-113 glutathione S-transferase kappa 1 Homo sapiens 4-7 7557435-2 1995 The vectors, pGEX-GTH and pET-HTG, produce protein fused to glutathione S-transferase (GST) at the N- and C-termini, respectively, allowing one-step purification on glutathione-Sepharose. Sepharose 177-186 glutathione S-transferase kappa 1 Homo sapiens 60-85 10092663-4 1999 Similarly, full-length [35S]mSec7-1/cytohesin was specifically adsorbed to glutathione-Sepharose loaded with glutathione S-transferase (GST)-ARP-Q79L, GST-ARP, or GST-ARP-T31N, the latter exhibiting the lowest binding affinity. Sepharose 87-96 glutathione S-transferase kappa 1 Homo sapiens 109-134 9400613-10 1997 Intraspecies PKR interactions were more efficient than interspecies PKR interactions, and interactions between RNA-binding-sufficient PKR proteins were more efficient than those involving an RNA-binding mutant as measured by binding to GST-PKR protein Sepharose beads. Sepharose 252-261 glutathione S-transferase kappa 1 Homo sapiens 236-239 9400613-12 1997 Purified mouse full-length PKR(1-515)WT GST fusion protein retained kinase activity on Sepharose beads, but the activity was not impaired by association with either the full-length or the N-terminal region of human PKR. Sepharose 87-96 glutathione S-transferase kappa 1 Homo sapiens 40-43 9171112-2 1997 In our assay, the protein is fused to the glutathione-S-transferase and bound to glutathione-Sepharose beads. Sepharose 93-102 glutathione S-transferase kappa 1 Homo sapiens 42-67 9343926-4 1997 When these fusion proteins (or GST), immobilized on glutathione-agarose beads were incubated with [35S] methionine labelled cell extracts, multiple proteins which interact specifically with SH3 domain of Hck were detected by SDS-PAGE followed by autoradiography. Sepharose 64-71 glutathione S-transferase kappa 1 Homo sapiens 31-34 8621443-11 1996 The GST-VEGF-exon 7 fusion protein bound to heparin-Sepharose with a similar affinity as VEGF165 and inhibited the binding of 125I-VEGF165 to 231 cells. Sepharose 52-61 glutathione S-transferase kappa 1 Homo sapiens 4-7 11353864-4 2001 Purification of GST-RyR3 was achieved by affinity chromatography by using glutathione-Sepharose. Sepharose 86-95 glutathione S-transferase kappa 1 Homo sapiens 16-19 10807041-4 2000 When glutathione S-transferase was purified by affinity chromatography on Sepharose-linked glutathione, incubated with lead chloride or lead acetate, a concentration-dependent inhibition of the enzymatic activity was observed reaching 50% inhibition at a lead salt concentration of 6000 microg/dl. Sepharose 74-83 glutathione S-transferase kappa 1 Homo sapiens 5-30 10082391-2 1999 The induced intracellular glutathione S-transferase (GST) fusion proteins of HBeAg-MV and HBeAg-SV were recovered and purified from bacterial lysates by affinity chromatography with glutathione-sepharose beads. Sepharose 194-203 glutathione S-transferase kappa 1 Homo sapiens 26-51 10082391-2 1999 The induced intracellular glutathione S-transferase (GST) fusion proteins of HBeAg-MV and HBeAg-SV were recovered and purified from bacterial lysates by affinity chromatography with glutathione-sepharose beads. Sepharose 194-203 glutathione S-transferase kappa 1 Homo sapiens 53-56 9792715-10 1998 The presence of 4 +/- 0.4 microM GST-DHPR II-III or 5 +/- 0.1 microM His-peptide-DHPR III-IV was required for half-maximal co-purification of 35S-labeled RyR1 Leu922-Asp1112 on glutathione-Sepharose or Ni2+-nitrilotriacetic acid. Sepharose 189-198 glutathione S-transferase kappa 1 Homo sapiens 33-36 8600179-5 1995 The GST/re-Hst1 fusion protein was isolated from cell lysates by affinity chromatography on glutathione (GSH)-Sepharose and digested with cyanogen bromide to separate re-Hst1 from the GST fusion partner. Sepharose 110-119 glutathione S-transferase kappa 1 Homo sapiens 4-7 7488288-9 1995 Selective removal of HRES-1 antibodies from sera of HRES-1-seropositive/RNP-seropositive patients by absorption on recombinant HRES-1/glutathione-S-transferase-conjugated agarose beads had no effect on anti-RNP reactivities. Sepharose 171-178 glutathione S-transferase kappa 1 Homo sapiens 134-159 7491122-2 1995 The GST-rAPEN fusion was subsequently overexpressed in Escherichia coli, purified on glutathione-agarose affinity columns, and the purified protein tested for AP endonuclease activity. Sepharose 97-104 glutathione S-transferase kappa 1 Homo sapiens 4-7 7629119-5 1995 Mutant GST fusion proteins that contain a single amino acid change (Y392S, Y392F, and Y392W) in the AIDA along with control GST were coupled to glutathione-Sepharose beads to form affinity beads. Sepharose 156-165 glutathione S-transferase kappa 1 Homo sapiens 7-10 7557435-2 1995 The vectors, pGEX-GTH and pET-HTG, produce protein fused to glutathione S-transferase (GST) at the N- and C-termini, respectively, allowing one-step purification on glutathione-Sepharose. Sepharose 177-186 glutathione S-transferase kappa 1 Homo sapiens 87-90 7925074-1 1994 Glutathione S-transferase (GST) with activity towards CDNB as a substrate from human intrauterine conceptual tissues (HICT) at 6-10 weeks of gestation was purified approximately 200-fold by GSH coupled Sepharose 4B affinity chromatography. Sepharose 202-214 glutathione S-transferase kappa 1 Homo sapiens 0-25 7822313-8 1995 Using GSH-Sepharose to selectively bind GST constructs, tightly bound kinase was shown to rapidly transfer in a highly preferential way from intact E2 core to GST constructs containing the E2L2 domain rather than to ones containing only the E2L1 domain. Sepharose 10-19 glutathione S-transferase kappa 1 Homo sapiens 40-43 7822313-8 1995 Using GSH-Sepharose to selectively bind GST constructs, tightly bound kinase was shown to rapidly transfer in a highly preferential way from intact E2 core to GST constructs containing the E2L2 domain rather than to ones containing only the E2L1 domain. Sepharose 10-19 glutathione S-transferase kappa 1 Homo sapiens 159-162 7822313-9 1995 GST-E2L2-kinase complexes could be eluted from GSH-Sepharose with glutathione. Sepharose 51-60 glutathione S-transferase kappa 1 Homo sapiens 0-3 7957681-3 1994 A recombinant human wild type p53 fused with glutathione S-transferase was immobilized on glutathione-agarose as a ligand for affinity column. Sepharose 102-109 glutathione S-transferase kappa 1 Homo sapiens 45-70 7925074-1 1994 Glutathione S-transferase (GST) with activity towards CDNB as a substrate from human intrauterine conceptual tissues (HICT) at 6-10 weeks of gestation was purified approximately 200-fold by GSH coupled Sepharose 4B affinity chromatography. Sepharose 202-214 glutathione S-transferase kappa 1 Homo sapiens 27-30 8097673-2 1993 We purified GST from human placenta using drug affinity chromatography on a column of W-77 coupled with Sepharose 6B and demonstrated that W-77 bound to GST. Sepharose 104-113 glutathione S-transferase kappa 1 Homo sapiens 12-15 8053565-2 1994 The histidine-tagged protein A bound efficiently to iminodiacetic acid (IDA)-Sepharose loaded with Zn2+, and the GST-protein A was efficiently retained by glutathione-Sepharose. Sepharose 167-176 glutathione S-transferase kappa 1 Homo sapiens 113-116 8489015-5 1993 We provide methods for the purification of GST fusion proteins at analytical and preparative scales, and demonstrate that saturation of glutathione agarose is dependent on fusion protein molecular weight. Sepharose 148-155 glutathione S-transferase kappa 1 Homo sapiens 43-46 1419639-2 1992 Enzymatic activity of GST in cytosols was measured by determining 1-chloro-2,4-dinitrobenzene conjugation with glutathione, cytosolic GST subunits were determined by wide pore reversed phase HPLC, using a S-hexylglutathione-agarose affinity column, and isoelectric focussing. Sepharose 224-231 glutathione S-transferase kappa 1 Homo sapiens 22-25 1449522-5 1992 GST purified from rat skin cytosol by GSH-agarose affinity chromatography exhibited a several-fold increase in the specific activity of enzyme with 1-chloro-2,4-dinitrobenzene (55-fold), ethacrynic acid (67-fold) and LTA4-methyl ester (12-fold) as substrates. Sepharose 42-49 glutathione S-transferase kappa 1 Homo sapiens 0-3 1713213-5 1991 The hybrid GST-Pim-1 fusion protein was affinity purified on a glutathione-Sepharose column prior to treatment with thrombin for cleavage of the Pim-1 protein from the transferase. Sepharose 75-84 glutathione S-transferase kappa 1 Homo sapiens 11-14 1527021-5 1992 A quantitative assay was developed which rapidly measured the ability of wild-type or mutant glutathione S-transferase to bind to glutathione-agarose. Sepharose 142-149 glutathione S-transferase kappa 1 Homo sapiens 93-118 1608942-5 1992 A c-Jun kinase activity was affinity-purified 5000-fold by using glutathione S-transferase-c-Jun-glutathione-Sepharose beads and was found to phosphorylate the N terminus of c-Jun but not v-Jun or c-Jun containing a 27-amino acid N-terminal deletion found in v-Jun. Sepharose 109-118 glutathione S-transferase kappa 1 Homo sapiens 65-90 1705771-2 1990 Human placental glutathione S-transferase was purified to apparent homogeneity by direct application of the crude homogenate into glutathione linked sepharose affinity chromatography. Sepharose 149-158 glutathione S-transferase kappa 1 Homo sapiens 16-41 2025229-7 1991 During the purification of GSTs with the use of affinity chromatography on GSH linked to epoxy-activated Sepharose 6B, FAEES and GST activities from each of these tissues segregated independently. Sepharose 105-114 glutathione S-transferase kappa 1 Homo sapiens 27-31 2025229-7 1991 During the purification of GSTs with the use of affinity chromatography on GSH linked to epoxy-activated Sepharose 6B, FAEES and GST activities from each of these tissues segregated independently. Sepharose 105-114 glutathione S-transferase kappa 1 Homo sapiens 27-30 2591027-2 1989 GSTs were purified from normal colon mucosa and from colonic tumours by affinity chromatography on glutathione-agarose. Sepharose 111-118 glutathione S-transferase kappa 1 Homo sapiens 0-4 34351836-3 2021 For this aim, the GST enzyme was purified from Vaccinium arctostapylous L. using the glutathione-agarose affinity chromatography and Sephadex G-100 gel filtration steps. Sepharose 97-104 glutathione S-transferase kappa 1 Homo sapiens 18-21 28153290-5 2017 The unpurified GST-hPPARgammaLBD was directly applied to a 96-well filter plate prepacked with glutathione sepharose. Sepharose 107-116 glutathione S-transferase kappa 1 Homo sapiens 15-18 32482903-2 2020 Glutathione immobilized on a chromatography matrix, such as agarose or Sepharose, acts as a substrate for the GST moiety of fusion proteins. Sepharose 60-67 glutathione S-transferase kappa 1 Homo sapiens 110-113 32482903-2 2020 Glutathione immobilized on a chromatography matrix, such as agarose or Sepharose, acts as a substrate for the GST moiety of fusion proteins. Sepharose 71-80 glutathione S-transferase kappa 1 Homo sapiens 110-113 19378031-12 2009 GST-pulldown experiments are similar in principle to Co-IPs, but a bait GST-fusion protein complexed to glutathione-sepharose (GSH) beads is used to pull down interaction partners instead of an antibody. Sepharose 116-125 glutathione S-transferase kappa 1 Homo sapiens 72-75 24337186-0 2014 An alternative easy method for antibody purification and analysis of protein-protein interaction using GST fusion proteins immobilized onto glutathione-agarose. Sepharose 152-159 glutathione S-transferase kappa 1 Homo sapiens 103-106 24337186-5 2014 The protocol for immobilization of GST-SPINK3 to glutathione-agarose beads was modified from previously reported protocols by using an alternative bifunctional cross-linker (dithiobis(succinimidyl propionate)) in a very simple procedure and by using simple buffers under physiological conditions. Sepharose 61-68 glutathione S-transferase kappa 1 Homo sapiens 35-38 22803665-2 2013 GST was purified 3089 fold with a specific activity of 20 U/mg and a yield of 78% from gastric tumour tissue; and 1185 fold with a specific activity of 5.69 U/mg and a yield of 50% from nontumour tissue by using glutathione-agarose affinity column, respectively. Sepharose 224-231 glutathione S-transferase kappa 1 Homo sapiens 0-3 19726331-4 2009 The fusion protein GST-Id-2 expressed in E. coli following IPTG induction was purified by glutathione-agarose affinity chromatography and used to immunize rabbits to prepare the polyclonal antibodies against GST-Id-2. Sepharose 102-109 glutathione S-transferase kappa 1 Homo sapiens 19-22 27063248-6 2016 Here, the affinity of GST for GSH was used to generate an enzyme-substrate site-specific cross-linking reaction; GSH-Sepharose was preactivated with 1-ethyl-3-(dimethylaminopropyl)carbodiimide (EDC) and then incubated Fc gamma receptor IIIa (FcgammaRIIIa)-GST. Sepharose 117-126 glutathione S-transferase kappa 1 Homo sapiens 22-25 27063248-6 2016 Here, the affinity of GST for GSH was used to generate an enzyme-substrate site-specific cross-linking reaction; GSH-Sepharose was preactivated with 1-ethyl-3-(dimethylaminopropyl)carbodiimide (EDC) and then incubated Fc gamma receptor IIIa (FcgammaRIIIa)-GST. Sepharose 117-126 glutathione S-transferase kappa 1 Homo sapiens 256-259 22703118-10 2012 A pull-down assay with glutathione S-transferase (GST)-agarose beads followed by Western blot analysis was employed to confirm microtubule S-glutathionylation. Sepharose 55-62 glutathione S-transferase kappa 1 Homo sapiens 23-48 22703118-10 2012 A pull-down assay with glutathione S-transferase (GST)-agarose beads followed by Western blot analysis was employed to confirm microtubule S-glutathionylation. Sepharose 55-62 glutathione S-transferase kappa 1 Homo sapiens 50-53 21081038-6 2010 The GST-TLE1-Q(1-136) fusion protein was induced by IPTG, digested by Thrombin, purified with glutathione-sepharose beads and FPLC, identified by SDS-PAGE. Sepharose 106-115 glutathione S-transferase kappa 1 Homo sapiens 4-7 20078429-3 2010 We demonstrate for the first time that this combination of three detergents significantly improves binding efficiency of GST and GST fusion proteins to gluthathione (GSH) Sepharose. Sepharose 171-180 glutathione S-transferase kappa 1 Homo sapiens 121-124 20078429-3 2010 We demonstrate for the first time that this combination of three detergents significantly improves binding efficiency of GST and GST fusion proteins to gluthathione (GSH) Sepharose. Sepharose 171-180 glutathione S-transferase kappa 1 Homo sapiens 129-132 16773246-0 2006 Identification of a glutathione S-transferase without affinity for glutathione sepharose in human kidney. Sepharose 79-88 glutathione S-transferase kappa 1 Homo sapiens 20-45 18775457-5 2008 As a result, using this GST:DEVD:EGFP reporter, caspase-3 activation based on proteolytic properties could be monitored via a variety of bioanalytical techniques such as immunoblot analysis, glutathione-agarose bead assay, and on-chip visualization, providing both technical and economical advantages over the extensively utilized fluorogenic peptide assay. Sepharose 203-210 glutathione S-transferase kappa 1 Homo sapiens 24-27 18662664-6 2008 The binding of GST-Gal1(N46D) to asialofetuin-Sepharose was less than 10% of that observed for GST-Gal1(WT), indicating that the mutant was deficient in carbohydrate-binding activity. Sepharose 46-55 glutathione S-transferase kappa 1 Homo sapiens 15-18 18491301-3 2008 The GST fusion protein is easily purified by affinity chromatography using a glutathione-Sepharose matrix under mild conditions. Sepharose 89-98 glutathione S-transferase kappa 1 Homo sapiens 4-7 18446053-3 2008 The ability of the proteins to form in vitro protein-DNA complexes was analyzed on agarose gel; both GST-Hoxc8(1-242) and GST-Hoxc8(149-208) formed complexes. Sepharose 83-90 glutathione S-transferase kappa 1 Homo sapiens 101-104