PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9531454-4 1998 Polymerase chain reaction using "hot start" and restriction enzyme digestion by HhaI was used for genotyping of apoE alleles, which were detected by polyacrylamide or MetaPhor agarose gel. Sepharose 176-183 apolipoprotein E Homo sapiens 112-116 14734213-3 2004 We studied the frequencies of the apoE alleles and genotypes in the three ethnic groups-Malay, Chinese and Indian-in Malaysia using DNA amplification followed by agarose gel electrophoresis. Sepharose 162-169 apolipoprotein E Homo sapiens 34-38 12684504-5 2003 Hybrid apolipoprotein and apoE3-N-terminal, but not apoLp-III, bound to heparin-Sepharose. Sepharose 80-89 apolipoprotein E Homo sapiens 7-21 12684504-5 2003 Hybrid apolipoprotein and apoE3-N-terminal, but not apoLp-III, bound to heparin-Sepharose. Sepharose 80-89 apolipoprotein E Homo sapiens 26-31 11880117-3 2002 Plasma lipids of pre- and post-LDL-apheresis were measured and apolipoprotein E (apoE) localization of the pre- and post-LDL-apheresis was detected by agarose gel electrophoresis. Sepharose 151-158 apolipoprotein E Homo sapiens 63-79 11880117-3 2002 Plasma lipids of pre- and post-LDL-apheresis were measured and apolipoprotein E (apoE) localization of the pre- and post-LDL-apheresis was detected by agarose gel electrophoresis. Sepharose 151-158 apolipoprotein E Homo sapiens 81-85 11880117-8 2002 Plasma apolipoprotein E detected between the prebeta- and alpha-mobility was markedly lower after the LDL-apheresis in the agarose gel electrophoresis. Sepharose 123-130 apolipoprotein E Homo sapiens 7-23 11910554-4 2002 Genotyping of polymorphic APOE alleles was done after polymerase chain reaction amplification of genomic DNA, digestion with HhaI, and agarose gel electrophoresis. Sepharose 135-142 apolipoprotein E Homo sapiens 26-30 20300302-5 2008 The apo E gene polymorphisms were determined by agarose gel electrophoresis. Sepharose 48-55 apolipoprotein E Homo sapiens 4-9 8776760-7 1996 The recombinant apoE isoforms were purified, under denaturating conditions, in one step by affinity chromatography on a Ni-chelated agarose column, yielding to about 20 mg of 96% pure protein per liter of culture. Sepharose 132-139 apolipoprotein E Homo sapiens 16-20 9192073-7 1997 Recombinant apoE3(1-183) was isolated by a combination of heparin-Sepharose chromatography and reverse-phase HPLC. Sepharose 66-75 apolipoprotein E Homo sapiens 12-17 12215771-6 1997 In addition it could bind on the heparin-Sepharose affinity chromatography column as Apo-E. Sepharose 41-50 apolipoprotein E Homo sapiens 85-90 7813084-0 1995 Apolipoprotein E2/E3/E4 genotyping with agarose gels. Sepharose 40-47 apolipoprotein E Homo sapiens 0-17 7600689-0 1995 Apolipoprotein E genotyping on agarose gels. Sepharose 31-38 apolipoprotein E Homo sapiens 0-16 2050696-8 1991 The apoE3 dimer displayed a preference for high density lipoproteins, as determined by agarose chromatography of E3/3 plasma but was stripped from high density lipoproteins by ultracentrifugation. Sepharose 87-94 apolipoprotein E Homo sapiens 4-9 7822240-5 1994 Apolipoprotein (apo) E-free HDL2 from the patients, separated by heparin-Sepharose column chromatography, was rich in CE, poor in triglycerides (TG), and enlarged in size on 4-30% nondenaturing polyacrylamide gradient gel electrophoresis. Sepharose 73-82 apolipoprotein E Homo sapiens 0-22 9222865-5 1994 Agarose column chromatography and gradient gel electrophoresis indicated that alpha-apoE belongs to early fractionated HDL, and that the precipitatable alpha-ApoE belongs to the higher molecular size HDL alpha-ApoE (%) estimated by immunofixation showed a strong positive correlation with apoE (%) in pHDL-fr. Sepharose 0-7 apolipoprotein E Homo sapiens 84-88 8111962-2 1993 A subfraction of HDL enriched in apolipoprotein E (apo E), separated by heparin-Sepharose affinity chromatography, was present in lower concentrations (P < 0.001) in the plasma of the coronary patients than in the control subjects. Sepharose 80-89 apolipoprotein E Homo sapiens 33-49 8111962-2 1993 A subfraction of HDL enriched in apolipoprotein E (apo E), separated by heparin-Sepharose affinity chromatography, was present in lower concentrations (P < 0.001) in the plasma of the coronary patients than in the control subjects. Sepharose 80-89 apolipoprotein E Homo sapiens 51-56 1718450-6 1991 Monoclonal antibody 3D12F11 (subclass IgG1) showed a high affinity for the apoE (Kd = 3.5 +/- 0.5 nM) without any effect on the apoprotein binding to heparin-Sepharose and apoE-induced destruction of dipalmitoylphosphatidylcholine liposomes. Sepharose 158-167 apolipoprotein E Homo sapiens 75-79 1551903-3 1992 Determination of the distribution of apoE among media lipoproteins by agarose column chromatography showed that the majority of secreted apoE was associated with large lipoproteins when cells were incubated with fetal bovine serum. Sepharose 70-77 apolipoprotein E Homo sapiens 37-41 1730728-6 1992 These two apoE variants were purified from cell lysates of the transfected Escherichia coli by ultracentrifugal flotation in the presence of phospholipid, by gel filtration chromatography, and by heparin-Sepharose chromatography. Sepharose 204-213 apolipoprotein E Homo sapiens 10-14 1795446-8 1991 The author recently reported that the apo C of high-density lipoprotein (HDL-apo C) was detected in alpha lipoprotein, but that HDL-apo E was detected in the near alpha 2-globulin region behind alpha lipoprotein on agarose-gel immunofixation electrophoresis. Sepharose 215-222 apolipoprotein E Homo sapiens 132-137 2340826-1 1990 A simple agarose isoelectric focusing gel method for apolipoprotein E phenotyping. Sepharose 9-16 apolipoprotein E Homo sapiens 53-69 2072046-0 1991 Rapid apolipoprotein E phenotyping by immunofixation in agarose. Sepharose 56-63 apolipoprotein E Homo sapiens 6-22 3619018-0 1987 Determination of apolipoprotein variants by isoelectric focusing in agarose. Sepharose 68-75 apolipoprotein E Homo sapiens 17-31 2791274-0 1989 Apolipoprotein E phenotype determined by agarose gel electrofocusing and immunoblotting. Sepharose 41-48 apolipoprotein E Homo sapiens 0-16 3395272-10 1988 Apo E also binds to the agarose-proteoglycan. Sepharose 24-31 apolipoprotein E Homo sapiens 0-5 3606467-4 1987 After separation of plasma lipoproteins by 4% agarose chromatography, an increased mass of apo E in lipoproteins of intermediate size was present; this may reflect the absence of LDL receptors that normally mediate their clearance. Sepharose 46-53 apolipoprotein E Homo sapiens 91-96 3619018-2 1987 In this paper we describe the use of agarose/urea as a focusing medium for IEF of apolipoproteins. Sepharose 37-44 apolipoprotein E Homo sapiens 82-97 3767285-0 1986 A method for the identification of apolipoprotein E isoforms employing chemical precipitation and flat bed isoelectric focusing in agarose. Sepharose 131-138 apolipoprotein E Homo sapiens 35-51 3100107-3 1986 This allowed measurement of apolipoproteins in lipidemic sera by SRID in agarose gel. Sepharose 73-80 apolipoprotein E Homo sapiens 28-43 3528366-4 1986 Residual apoE and albumin, amounting up to 0.5% of the apoB mass, were resistant to removal by TGRP treatment as well as by heparin-Sepharose column chromatography. Sepharose 132-141 apolipoprotein E Homo sapiens 9-13 3005328-5 1986 The apo-E receptor, which did not bind to the LDL-Sepharose column, was then purified by using an HDLc (cholesterol-induced high density lipoprotein)-Sepharose affinity column and an immunoaffinity column. Sepharose 150-159 apolipoprotein E Homo sapiens 4-9 3909150-3 1985 The bacterially produced apoE was purified by heparin-Sepharose affinity chromatography, Sephacryl S-300 gel filtration, and preparative Immobiline isoelectric focusing. Sepharose 54-63 apolipoprotein E Homo sapiens 25-29 2418019-2 1986 The interaction of human apolipoprotein (apo-) E3 with heparin was examined using heparin-Sepharose as a model system. Sepharose 90-99 apolipoprotein E Homo sapiens 25-48 3924105-1 1985 Discrete apolipoprotein E-containing lipoproteins can be identified when EDTA plasma is fractionated on columns of 4% agarose. Sepharose 118-125 apolipoprotein E Homo sapiens 9-25 3840034-7 1985 The apoE mRNAs appear to be intact and migrate on an agarose gel under denaturing conditions at approximately 18 S. To assay for the biological activity of the apoE mRNAs in these tissues, they were translated in a reticulocyte lysate system in vitro. Sepharose 53-60 apolipoprotein E Homo sapiens 4-8 6207956-3 1984 In a more detailed analysis of three subjects, we measured the lipoprotein association of apo E by column chromatography on agarose beads, before and after its precipitation from plasma. Sepharose 124-131 apolipoprotein E Homo sapiens 90-95 3988735-3 1985 Both apo-C-II and apo-E produced enhanced lipolysis in comparison to unsupplemented emulsions, at appropriate enzyme densities on the heparin-Sepharose. Sepharose 142-151 apolipoprotein E Homo sapiens 18-23 3988735-6 1985 The enhancement of lipolysis produced by apo-E was correlated with the increased binding of triglyceride to the heparin-Sepharose enzyme complex. Sepharose 120-129 apolipoprotein E Homo sapiens 41-46 6480826-5 1984 The new series of apo E components, named apo E-Suita, was identical with the ordinary apo E in its interaction with heparin-Sepharose gel and with anti-apo E antibody. Sepharose 125-134 apolipoprotein E Homo sapiens 18-23 6480826-5 1984 The new series of apo E components, named apo E-Suita, was identical with the ordinary apo E in its interaction with heparin-Sepharose gel and with anti-apo E antibody. Sepharose 125-134 apolipoprotein E Homo sapiens 42-47 6480826-5 1984 The new series of apo E components, named apo E-Suita, was identical with the ordinary apo E in its interaction with heparin-Sepharose gel and with anti-apo E antibody. Sepharose 125-134 apolipoprotein E Homo sapiens 42-47 6480826-5 1984 The new series of apo E components, named apo E-Suita, was identical with the ordinary apo E in its interaction with heparin-Sepharose gel and with anti-apo E antibody. Sepharose 125-134 apolipoprotein E Homo sapiens 42-47 7440713-2 1980 ApoE was purified from the very low density lipoproteins of hypertriglyceridemic patients by heparin-agarose affinity chromatography, DEAE-cellulose chromatography, and preparative polyacrylamide gel electrophoresis. Sepharose 101-108 apolipoprotein E Homo sapiens 0-4 6712769-4 1984 The new apolipoprotein component, named apo E-5, was identical with ordinary apo E in apparent molecular weight by SDS-polyacrylamide gel electrophoresis and in its interactions with heparin-Sepharose gel and with anti-apo E antibody. Sepharose 191-200 apolipoprotein E Homo sapiens 40-45 7161560-4 1982 The portion of apoE associated with triglyceride-rich lipoproteins as assessed by agarose column chromatography increased by a mean of 44%. Sepharose 82-89 apolipoprotein E Homo sapiens 15-19 7318173-6 1981 (3) When plasma was subjected to gel filtration on columns of 6% agarose, apolipoprotein E was located in three regions. Sepharose 65-72 apolipoprotein E Homo sapiens 74-90 7440713-13 1980 The lipoprotein distribution of apoE was investigated by agarose column chromatography and ultracentrifugation of plasma. Sepharose 57-64 apolipoprotein E Homo sapiens 32-36 7440713-14 1980 Agarose column chromatography demonstrated that all or nearly all plasma apoE is associated with lipoproteins. Sepharose 0-7 apolipoprotein E Homo sapiens 73-77 182242-2 1976 Apolipoprotein E ("arginine-rich" polypeptide) was isolated from delipidized human very low density lipoproteins by agarose column chromatography in the presence of 6 M guanidine-hydrochloride. Sepharose 116-123 apolipoprotein E Homo sapiens 0-16