PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15864429-5 2005 The MBP-tagged enzyme was efficiently purified by a combination of cation-exchange column and amylase-conjugated agarose column chromatography. Sepharose 113-120 myelin basic protein Homo sapiens 4-7 7681451-4 1993 IgG was purified from free protein extracts by protein G Sepharose affinity chromatography and anti-MBP was further isolated from purified IgG by antigen specific (MBP) Sepharose affinity chromatography. Sepharose 169-178 myelin basic protein Homo sapiens 100-103 14751262-3 2004 The small size of CaM hinders its immobilization in low-weight-percentage agarose gels; however, fusion of CaM to MBP via a flexible linker provides sufficient restriction of translational mobility in 1% agarose gels. Sepharose 204-211 myelin basic protein Homo sapiens 114-117 8175758-4 1994 The p15cdk-BP-bound "PSTAIRE signal" is part of a 250-kDa complex distinct from p34cdc2/cyclin B. p15cdk-BP-Sepharose beads retain a kinase phosphorylating HMG I/Y, P1, and myelin basic protein (among 24 substrates tested). Sepharose 108-117 myelin basic protein Homo sapiens 173-193 7515696-1 1994 To study the relationship between a bovine serum mannan-binding protein (MBP) and a serum protein reactive with a Ra chemotype strain of Salmonella serovar Typhimurium (Ra-reactive factor, RaRF), both proteins were isolated by use of their affinity for yeast mannan and the Salmonella cells followed by affinity chromatography on mannobiose-Sepharose 4B. Sepharose 341-350 myelin basic protein Homo sapiens 49-71 7683331-5 1993 Anti-MBP was isolated from purified IgG from brain and spinal cord by MBP-Sepharose affinity chromatography. Sepharose 74-83 myelin basic protein Homo sapiens 5-8 2313094-1 1990 The serum lectin, mannan binding protein (MBP), was isolated in a yield of 40 micrograms/liter from pooled normal human serum by affinity chromatography on mannan-Sepharose, followed by gel-filtration and ion-exchange chromatography and finally by passage down an anti-IgM Sepharose column. Sepharose 163-172 myelin basic protein Homo sapiens 18-40 1460414-3 1992 The human serum MBP fraction was obtained by sequential affinity chromatography on mannan-Sepharose, anti-IgM-Sepharose and anti-MBP-Sepharose in the presence of calcium ions. Sepharose 90-99 myelin basic protein Homo sapiens 16-19 1460414-3 1992 The human serum MBP fraction was obtained by sequential affinity chromatography on mannan-Sepharose, anti-IgM-Sepharose and anti-MBP-Sepharose in the presence of calcium ions. Sepharose 110-119 myelin basic protein Homo sapiens 16-19 1460414-3 1992 The human serum MBP fraction was obtained by sequential affinity chromatography on mannan-Sepharose, anti-IgM-Sepharose and anti-MBP-Sepharose in the presence of calcium ions. Sepharose 110-119 myelin basic protein Homo sapiens 16-19 1460414-5 1992 The C1s-like serine protease, designated MBP-associated serine protease (MASP), was separated from MBP by rechromatography on anti-MBP-Sepharose in the presence of ethylenediaminetetraacetic acid. Sepharose 135-144 myelin basic protein Homo sapiens 41-44 1373999-6 1992 Antibodies to MBP were isolated from purified CSF IgG of MS patients with acute relapses by two-step antigen specific (MBP-Sepharose) affinity chromatography. Sepharose 123-132 myelin basic protein Homo sapiens 14-17 1373999-6 1992 Antibodies to MBP were isolated from purified CSF IgG of MS patients with acute relapses by two-step antigen specific (MBP-Sepharose) affinity chromatography. Sepharose 123-132 myelin basic protein Homo sapiens 119-122 2313094-1 1990 The serum lectin, mannan binding protein (MBP), was isolated in a yield of 40 micrograms/liter from pooled normal human serum by affinity chromatography on mannan-Sepharose, followed by gel-filtration and ion-exchange chromatography and finally by passage down an anti-IgM Sepharose column. Sepharose 163-172 myelin basic protein Homo sapiens 42-45 2313094-1 1990 The serum lectin, mannan binding protein (MBP), was isolated in a yield of 40 micrograms/liter from pooled normal human serum by affinity chromatography on mannan-Sepharose, followed by gel-filtration and ion-exchange chromatography and finally by passage down an anti-IgM Sepharose column. Sepharose 273-282 myelin basic protein Homo sapiens 18-40 2313094-1 1990 The serum lectin, mannan binding protein (MBP), was isolated in a yield of 40 micrograms/liter from pooled normal human serum by affinity chromatography on mannan-Sepharose, followed by gel-filtration and ion-exchange chromatography and finally by passage down an anti-IgM Sepharose column. Sepharose 273-282 myelin basic protein Homo sapiens 42-45 2313094-4 1990 MBP, after interaction with zymosan, caused efficient activation of a C1r2 125I-C1s2 complex that was prepared by incubation of 125I-C1s2 with serum, from a patient with a complete genetic deficiency of C1q, followed by gel-filtration on Sepharose 6B. Sepharose 238-247 myelin basic protein Homo sapiens 0-3 2442667-1 1987 Migration properties and occurrence of antibodies against myelin basic protein (MBP) in paired CSF and serum specimens from patients with multiple sclerosis (MS) were demonstrated after agarose isoelectric focusing, immunoblot transfer, and immunoperoxidase staining. Sepharose 186-193 myelin basic protein Homo sapiens 80-83 30112774-4 2019 Approximately 82% electrophoretically homogeneous SCZ IgGs purified using several affinity sorbents including Sepharose with immobilized MBP hydrolyze specifically only MBP but not many other tested proteins. Sepharose 110-119 myelin basic protein Homo sapiens 169-172 6083471-1 1984 Two different kinds of immunosorbents were prepared that contained the synthetic myelin basic protein didecapeptide S82 (TTHYGSLPQKAQGHRDQDEG)--one coupled with AH-Sepharose 4B through hexanoate spacers to the C-terminal glycyl residue; the other, with CH-Sepharose 4B through hexanoate spacers to the N-terminal threonine residue. Sepharose 164-173 myelin basic protein Homo sapiens 81-101 6083471-1 1984 Two different kinds of immunosorbents were prepared that contained the synthetic myelin basic protein didecapeptide S82 (TTHYGSLPQKAQGHRDQDEG)--one coupled with AH-Sepharose 4B through hexanoate spacers to the C-terminal glycyl residue; the other, with CH-Sepharose 4B through hexanoate spacers to the N-terminal threonine residue. Sepharose 256-265 myelin basic protein Homo sapiens 81-101 6165382-6 1981 Complete equilibrium binding isotherms of both detergents to the protein were obtained by using MBP immobilized on agarose. Sepharose 115-122 myelin basic protein Homo sapiens 96-99 6165382-10 1981 Affinity chromatography studies indicated that, in the presence of NaDodSO4 (but not in its absence), [125I]MBP interacted with agarose-immobilized histone, lysozyme, and MBP but did not interact with ovalbumin-agarose. Sepharose 128-135 myelin basic protein Homo sapiens 108-111 6165382-10 1981 Affinity chromatography studies indicated that, in the presence of NaDodSO4 (but not in its absence), [125I]MBP interacted with agarose-immobilized histone, lysozyme, and MBP but did not interact with ovalbumin-agarose. Sepharose 211-218 myelin basic protein Homo sapiens 108-111 27730557-2 2017 MBP allows the use of a simple capture affinity step on Amylose-Agarose or Dextrin-Sepharose columns, resulting in a protein that is often 70-90 % pure in a single step. Sepharose 64-71 myelin basic protein Homo sapiens 0-3 27730557-2 2017 MBP allows the use of a simple capture affinity step on Amylose-Agarose or Dextrin-Sepharose columns, resulting in a protein that is often 70-90 % pure in a single step. Sepharose 83-92 myelin basic protein Homo sapiens 0-3 23520443-1 2013 IgGs from patients with multiple sclerosis and systemic lupus erythematosus (SLE) purified on MBP-Sepharose in contrast to canonical proteases hydrolyze effectively only myelin basic protein (MBP), but not many other tested proteins. Sepharose 98-107 myelin basic protein Homo sapiens 94-97 23520443-1 2013 IgGs from patients with multiple sclerosis and systemic lupus erythematosus (SLE) purified on MBP-Sepharose in contrast to canonical proteases hydrolyze effectively only myelin basic protein (MBP), but not many other tested proteins. Sepharose 98-107 myelin basic protein Homo sapiens 170-190 23520443-1 2013 IgGs from patients with multiple sclerosis and systemic lupus erythematosus (SLE) purified on MBP-Sepharose in contrast to canonical proteases hydrolyze effectively only myelin basic protein (MBP), but not many other tested proteins. Sepharose 98-107 myelin basic protein Homo sapiens 192-195 18855760-2 2008 The soluble fusion protein MBP-Gly1-Gln26-rhPTH(1-34) was harvested after purification by Phenyl-Sepharose F.F and Q-Sepharose F.F chromatographies. Sepharose 97-106 myelin basic protein Homo sapiens 27-30 22781164-1 2012 In contrast to canonical proteases, myelin basic protein (MBP)-Sepharose-purified IgG from multiple sclerosis (MS) and systemic lupus erythematosus (SLE) patients efficiently hydrolyze only MBP, but not many other tested proteins. Sepharose 63-72 myelin basic protein Homo sapiens 36-56 22781164-1 2012 In contrast to canonical proteases, myelin basic protein (MBP)-Sepharose-purified IgG from multiple sclerosis (MS) and systemic lupus erythematosus (SLE) patients efficiently hydrolyze only MBP, but not many other tested proteins. Sepharose 63-72 myelin basic protein Homo sapiens 58-61 22781164-1 2012 In contrast to canonical proteases, myelin basic protein (MBP)-Sepharose-purified IgG from multiple sclerosis (MS) and systemic lupus erythematosus (SLE) patients efficiently hydrolyze only MBP, but not many other tested proteins. Sepharose 63-72 myelin basic protein Homo sapiens 190-193 22434709-4 2012 A similar situation was observed for IgG from patients with multiple sclerosis and HIV-infected patients, which after purification on myelin basic protein (MBP)-Sepharose and RT-Sepharose specifically hydrolyze only MBP and RT, respectively. Sepharose 161-170 myelin basic protein Homo sapiens 134-154 22434709-4 2012 A similar situation was observed for IgG from patients with multiple sclerosis and HIV-infected patients, which after purification on myelin basic protein (MBP)-Sepharose and RT-Sepharose specifically hydrolyze only MBP and RT, respectively. Sepharose 161-170 myelin basic protein Homo sapiens 156-159 22434709-4 2012 A similar situation was observed for IgG from patients with multiple sclerosis and HIV-infected patients, which after purification on myelin basic protein (MBP)-Sepharose and RT-Sepharose specifically hydrolyze only MBP and RT, respectively. Sepharose 178-187 myelin basic protein Homo sapiens 216-219 22038803-2 2011 Approximately 86% electrophoretically and immunologically homogeneous SLE immunoglobulin Gs (IgGs) purified using several affinity resins including Sepharose with immobilized hMBP specifically hydrolyze only hMBP but not many other tested proteins. Sepharose 148-157 myelin basic protein Homo sapiens 208-212 20978971-2 2011 MBP allows one to use a simple capture affinity step on amylose-agarose columns, resulting in a protein that is often 70-90% pure. Sepharose 64-71 myelin basic protein Homo sapiens 0-3 16310860-7 2006 Ni(2+)-activated IgGs were separated into distinct MBP-hydrolyzing fractions by chromatography on HiTraptrade mark Chelating Sepharose charged with Ni(2+). Sepharose 125-134 myelin basic protein Homo sapiens 51-54 15978327-5 2005 The soluble form of MBP-Ta60b fused scFv could be extracted and affinity-purified with an amylose/agarose column, allowing its immunoreactivity to be analyzed by enzyme-linked immunosorbent assay (ELISA), mixed hemadsorption assay, and fluorescence activated cell sorting. Sepharose 98-105 myelin basic protein Homo sapiens 20-23