PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2571074-5 1989 Heparin-releasable LPL could be resolved into two fractions by chromatography on con A-Sepharose; this pattern of elution was not affected by the prior treatment of cardiac myocytes with taxol. Sepharose 87-96 lipoprotein lipase Homo sapiens 19-22 3355847-5 1988 Furthermore, when postheparin plasma was mixed with monoclonal antibody prior to gel filtration on 6% agarose, the LPL activity eluted with the lipoproteins and was not inhibited by the antibody. Sepharose 102-109 lipoprotein lipase Homo sapiens 115-118 3606717-2 1987 LPL from post-heparin plasma was first purified by heparin Sepharose 4B affinity chromatography. Sepharose 59-71 lipoprotein lipase Homo sapiens 0-3 6951202-4 1982 The enzyme was characterized as lipoprotein lipase (triacylglycero-protein acylhydrolase, EC 3.1.1.34) on the basis of pH optimum (7.8--8.2 for monocytes, 8.1 for alveolar macrophages), dependence on apolipoprotein C-II for activity, inhibition by 0.3--0.5 M sodium chloride and protamine sulfate, and retention of a heparin-Sepharose gel. Sepharose 325-334 lipoprotein lipase Homo sapiens 32-50 3756191-8 1986 First, post-heparin plasma lipoprotein lipase activity and immunoreactivity detected by an enzyme-linked immunosorbent assay (ELISA) co-eluted during heparin-agarose and phenyl-Sepharose chromatography. Sepharose 158-165 lipoprotein lipase Homo sapiens 27-45 3756191-8 1986 First, post-heparin plasma lipoprotein lipase activity and immunoreactivity detected by an enzyme-linked immunosorbent assay (ELISA) co-eluted during heparin-agarose and phenyl-Sepharose chromatography. Sepharose 176-186 lipoprotein lipase Homo sapiens 27-45 3994667-7 1985 Binding of active lipoprotein lipase to heparin-Sepharose could be demonstrated at pH down to 6.5. Sepharose 48-57 lipoprotein lipase Homo sapiens 18-36 3994667-11 1985 Catalytically inactive lipoprotein lipase retained the ability to bind to heparin-Sepharose. Sepharose 82-91 lipoprotein lipase Homo sapiens 23-41 865246-2 1977 Lipoprotein lipase and hepatic triglyceride lipase were differentiated by assay under high and low salt conditions and also by separation on heparin-agarose affinity chromatography columns. Sepharose 149-156 lipoprotein lipase Homo sapiens 0-18 75564-6 1978 These results indicate that the removal of antithrombin III is the major problem in the purification of H-TGL and LPL from human post-heparin plasma by heparin-Sepharose affinity chromatography. Sepharose 160-169 lipoprotein lipase Homo sapiens 114-117 884004-4 1977 Post heparin plasma lipoprotein lipase activity isolated and partially purified by heparin Sepharose affinity chromatography was determined quantitatively. Sepharose 91-100 lipoprotein lipase Homo sapiens 20-38 24984153-7 2014 One of the selected compounds, 50F10, was directly shown to preserve the active homodimer structure of LPL, as demonstrated by heparin-Sepharose chromatography. Sepharose 135-144 lipoprotein lipase Homo sapiens 103-106 1008906-4 1976 With heparin-Sepharose 4 B affinity chromatography it was possible to partially purify human adipose tissue lipoprotein lipase (LPL) as well as a lipase from human liver. Sepharose 13-22 lipoprotein lipase Homo sapiens 108-126 1008906-4 1976 With heparin-Sepharose 4 B affinity chromatography it was possible to partially purify human adipose tissue lipoprotein lipase (LPL) as well as a lipase from human liver. Sepharose 13-22 lipoprotein lipase Homo sapiens 128-131 8061-1 1976 Human heart lipoprotein lipase was purified by affinity chromatography on heparin-Sepharose 4B. Sepharose 82-94 lipoprotein lipase Homo sapiens 12-30 5059200-1 1972 When NH(4)OH-NH(4)Cl extracts of adipose acetone powder were applied to agarose gel chromatography columns, two peaks of lipoprotein lipase were eluted. Sepharose 72-79 lipoprotein lipase Homo sapiens 121-139 30850549-8 2019 We also used density gradient ultracentrifugation to characterize the LPL within the high-salt and low-salt peaks from a heparin-Sepharose column. Sepharose 129-138 lipoprotein lipase Homo sapiens 70-73 15385564-3 2004 Evidence that LPL dimers rapidly exchange subunits was demonstrated by fluorescence resonance energy transfer between lipase subunits labeled with Oregon Green and tetrametylrhodamine, respectively, and also by formation of heterodimers composed of radiolabeled and biotinylated lipase subunits captured on streptavidine-agarose. Sepharose 321-328 lipoprotein lipase Homo sapiens 14-17 24704550-8 2014 In the cell-free assay, we compared the binding of internally tagged WT-LPL and S447X-LPL to soluble GPIHBP1 immobilized on agarose beads. Sepharose 124-131 lipoprotein lipase Homo sapiens 86-89 9445371-6 1998 The study with a heparin-Sepharose column showed that 3T3-L1 adipocytes contained three forms of LPL. Sepharose 25-34 lipoprotein lipase Homo sapiens 97-100 14568190-0 2003 Tamoxifen might influence the affinity of LPL for heparin-sepharose. Sepharose 58-67 lipoprotein lipase Homo sapiens 42-45 14568190-3 2003 METHODS: Lipoprotein lipase in post-heparin plasma usually exists in both monomeric and dimeric forms, which may be separated on a heparin-Sepharose column with different salt concentrations. Sepharose 139-148 lipoprotein lipase Homo sapiens 9-27 14568190-4 2003 Lipoprotein lipase in post-heparin plasma from postmenopausal patients with hypertriglyceridemia treated with or without tamoxifen was incubated with or without 4-hydroxy-tamoxifen (4-OHT), the monomers and dimers were separated on a heparin-Sepharose column and their masses were measured. Sepharose 242-251 lipoprotein lipase Homo sapiens 0-18 14568190-6 2003 Monomeric LPL of tamoxifen-treated patients passed more slowly through the heparin-Sepharose column compared with that of control subjects. Sepharose 83-92 lipoprotein lipase Homo sapiens 10-13 14568190-8 2003 In addition, monomeric LPL incubated with 4-OHT passed more slowly through the heparin-Sepharose column compared with that incubated without 4-OHT. Sepharose 87-96 lipoprotein lipase Homo sapiens 23-26 12119116-10 2002 This residue is conserved in LPL from all mammals and has been shown to be critical for enzyme stability at 37 degrees C. On chromatography on heparin-Sepharose trout and chicken LPL eluted at higher salt concentration than bovine (or other mammalian) LPL. Sepharose 151-160 lipoprotein lipase Homo sapiens 29-32 9812994-7 1998 Heparin-Sepharose chromatography demonstrated that HL-LPLC1 and HL-LPLC2 eluted at 0.80 and 1.3 M NaCl, respectively, elution positions that corresponded to native HL and LPL. Sepharose 8-17 lipoprotein lipase Homo sapiens 54-57 12213490-5 2002 In the adipose tissue of the untreated group, 72% of the LPL was the inactive-monomeric form, which was eluted with 0.4-0.75 M NaCl from the heparin-Sepharose column, and 28% was the active-dimeric form, which was eluted with 0.8-1.2 M NaCl. Sepharose 149-158 lipoprotein lipase Homo sapiens 57-60 8773545-2 1996 They were subsequently chromatographed on a lipoprotein lipase (LpL)-Sepharose column. Sepharose 69-78 lipoprotein lipase Homo sapiens 64-67 9034202-7 1997 LDL binding to LPL containing heparin-agarose was also disrupted by the amino-terminal antibodies to apoB. Sepharose 38-45 lipoprotein lipase Homo sapiens 15-18 7811743-3 1995 Nearly all the LPL in post-heparin plasma of controls bound to heparin-Sepharose and this LPL bound was mainly eluted with 1.5 M NaCl in parallel with the activity. Sepharose 71-80 lipoprotein lipase Homo sapiens 15-18 7488211-3 1995 LPL-sepharose affinity chromatography of [35S]O4 labeled HAEC proteins identified a 220-kDa proteoglycan. Sepharose 4-13 lipoprotein lipase Homo sapiens 0-3 1644832-2 1992 Previous studies from this laboratory using LPL-Sepharose affinity chromatography identified a 220-kDa LPL binding proteoglycan. Sepharose 48-57 lipoprotein lipase Homo sapiens 44-47 8144523-8 1994 Using heparin-agarose affinity chromatography, a 116-kDa LPL-binding protein was purified from endothelial cell extracts. Sepharose 14-21 lipoprotein lipase Homo sapiens 57-60 8288243-6 1993 The mutated LPL protein was secreted from the cells in a manner similar to that of wild-type LPL and bound to heparin-Sepharose with identical properties. Sepharose 118-127 lipoprotein lipase Homo sapiens 12-15 8228638-5 1993 The LPL mass in preheparin plasma eluted early from heparin-Sepharose, in the position expected for inactive LPL monomers. Sepharose 60-69 lipoprotein lipase Homo sapiens 4-7 8228638-7 1993 The increment of mass and activity after heparin eluted later from heparin-Sepharose, in the position expected for active LPL dimers. Sepharose 75-84 lipoprotein lipase Homo sapiens 122-125 7516153-1 1994 The interaction between bovine lipoprotein lipase (bLPL) and human alpha 2-macroglobulin (alpha 2M) was studied by use of non-denaturing PAGE and gel-permeation, Zn(2+)-Sepharose and heparin-Sepharose chromatography. Sepharose 169-178 lipoprotein lipase Homo sapiens 31-49 1644832-6 1992 Furthermore, the biotinylated 116-kDa protein bound to LPL-Sepharose and eluted with 0.4 M NaCl suggesting that the 116-kDa LPL binding protein is present on the cell surface. Sepharose 59-68 lipoprotein lipase Homo sapiens 124-127 1644832-7 1992 When detergent extracts of endothelial cells were applied to LPL-Sepharose in the presence of 0.15 M NaCl, the 116-kDa, but not the 220-kDa, protein still bound to LPL-Sepharose. Sepharose 65-74 lipoprotein lipase Homo sapiens 61-64 1644832-7 1992 When detergent extracts of endothelial cells were applied to LPL-Sepharose in the presence of 0.15 M NaCl, the 116-kDa, but not the 220-kDa, protein still bound to LPL-Sepharose. Sepharose 168-177 lipoprotein lipase Homo sapiens 164-167 1279089-12 1992 The effect of conformation and dimeric structure on LPL-heparin interaction was studied by heparin-Sepharose chromatography. Sepharose 99-108 lipoprotein lipase Homo sapiens 52-55 1644832-2 1992 Previous studies from this laboratory using LPL-Sepharose affinity chromatography identified a 220-kDa LPL binding proteoglycan. Sepharose 48-57 lipoprotein lipase Homo sapiens 103-106 1644832-6 1992 Furthermore, the biotinylated 116-kDa protein bound to LPL-Sepharose and eluted with 0.4 M NaCl suggesting that the 116-kDa LPL binding protein is present on the cell surface. Sepharose 59-68 lipoprotein lipase Homo sapiens 55-58 1953677-9 1991 On lipoprotein lipase-agarose the endothelial heparan sulphate chains were eluted at the same salt concentration as heparin, and the binding persisted, although with decreased strength, after digestion with heparinase. Sepharose 22-29 lipoprotein lipase Homo sapiens 3-21 2110364-3 1990 Analysis of the patient"s post-heparin plasma by heparin-Sepharose affinity chromatography demonstrated that the mutant LPL had an altered affinity for heparin. Sepharose 57-66 lipoprotein lipase Homo sapiens 120-123 34780727-5 2021 For LPL purification, we used heparin-Sepharose affinity chromatography, which disrupted LPL-GPIHBP1 complexes causing GPIHBP1 to elute with the flow-through of the conditioned media. Sepharose 38-47 lipoprotein lipase Homo sapiens 89-92 2511018-3 1989 The patient"s LpL purified from the PHP by heparin-Sepharose and phenyl-Sepharose chromatographies hydrolysed tributryrin, but not triolein emulsified with Triton X-100 and phosphatidylcholine (PC), or in chylomicrons, whereas normal LpL hydrolysed these substrates. Sepharose 51-60 lipoprotein lipase Homo sapiens 14-17