PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11520413-2 2001 MATERIALS AND METHODS: A1PI was purified from Cohn fraction IV-1,4 using ethanol precipitation and Q-Sepharose chromatography. Sepharose 101-110 serpin family A member 1 Homo sapiens 23-27 23648095-7 2013 Finally, fibrin(ogen)-Sepharose chromatography indicated that A1AT purified from plasma contained a small fraction of fibrin(ogen)-binding A1AT. Sepharose 22-31 serpin family A member 1 Homo sapiens 62-66 19995544-5 2010 A highly purified alpha1-antitrypsin was isolated at 95% step recovery by adsorbing the flow-through on 4% epoxy-crosslinked agarose-10% tungsten carbide adsorbent material coupled with a cationic ligand. Sepharose 125-132 serpin family A member 1 Homo sapiens 18-36 6153632-3 1980 The complexes between elastase and alpha 1-antitrypsin and alpha 2-macroglobulin, respectively, migrate as alpha 2-globulin on agarose gel electrophoresis. Sepharose 127-134 serpin family A member 1 Homo sapiens 35-54 9769931-0 1998 [Determination of alpha 1 antitrypsin phenotypes in plasma using isoelectric focusing on this agarose gel]. Sepharose 94-101 serpin family A member 1 Homo sapiens 18-37 2208661-0 1990 Improved method for identifying alpha 1-antitrypsin Pi M subtypes by isoelectric focusing in agarose. Sepharose 93-100 serpin family A member 1 Homo sapiens 32-51 2208661-1 1990 We describe an improved method for the classification of alpha 1-antitrypsin variants by isoelectric focusing in agarose. Sepharose 113-120 serpin family A member 1 Homo sapiens 57-76 3485073-0 1986 Distribution of alpha-1-antitrypsin (Pi) phenotypes in Denmark determined by separator isoelectric focusing in agarose gel. Sepharose 111-118 serpin family A member 1 Homo sapiens 16-35 3485073-1 1986 The distribution of phenotypes of alpha 1-antitrypsin (Pi) in 909 unrelated Danes was determined by the use of separator isoelectric focusing in agarose gel. Sepharose 145-152 serpin family A member 1 Homo sapiens 34-53 3874722-0 1985 N-[(carbamoylmethyl)amino]ethanesulfonic acid improves phenotyping of alpha 1-antitrypsin by isoelectric focusing on agarose gel. Sepharose 117-124 serpin family A member 1 Homo sapiens 70-89 3874722-3 1985 I describe a method in which the ultrathin agarose gel contains N-[(carbamoylmethyl)amino]ethanesulfonic acid as a "separator," to flatten the pH gradient and improve separation of the alpha 1-antitrypsin isoforms. Sepharose 43-50 serpin family A member 1 Homo sapiens 185-204 3873300-0 1985 Phenotyping alpha-1-antitrypsin (alpha 1-AT) variants by isoelectric focusing in agarose and immunoblotting. Sepharose 81-88 serpin family A member 1 Homo sapiens 12-31 3873300-0 1985 Phenotyping alpha-1-antitrypsin (alpha 1-AT) variants by isoelectric focusing in agarose and immunoblotting. Sepharose 81-88 serpin family A member 1 Homo sapiens 33-43 6182004-3 1982 The inhibition was abolished by removal of urinary alpha1-antitrypsin by trypsin-sepharose treatment. Sepharose 81-90 serpin family A member 1 Homo sapiens 51-69 6980436-2 1982 AAT genetic phenotypes were determined using acid agarose gel electrophoresis, followed by crossed antigen-antibody electrophoresis in agarose gel. Sepharose 50-57 serpin family A member 1 Homo sapiens 0-3 6335631-0 1984 Affinity chromatography of alpha-1-protease inhibitor using Sepharose-4B-bound anhydrochymotrypsin. Sepharose 60-72 serpin family A member 1 Homo sapiens 27-53 6335631-1 1984 Sepharose 4B-bound bovine anhydrochymotrypsin (AnhCT), a catalytically inactive form of chymotrypsin, was shown to be effective for retaining active alpha-1-protease inhibitor (alpha-1-PI, also alpha-1-antitrypsin) from human plasma, while showing no measurable affinity for oxidized or protease complexed alpha-1-PI, or for most other plasma proteins. Sepharose 0-12 serpin family A member 1 Homo sapiens 149-175 6335631-1 1984 Sepharose 4B-bound bovine anhydrochymotrypsin (AnhCT), a catalytically inactive form of chymotrypsin, was shown to be effective for retaining active alpha-1-protease inhibitor (alpha-1-PI, also alpha-1-antitrypsin) from human plasma, while showing no measurable affinity for oxidized or protease complexed alpha-1-PI, or for most other plasma proteins. Sepharose 0-12 serpin family A member 1 Homo sapiens 177-187 6335631-1 1984 Sepharose 4B-bound bovine anhydrochymotrypsin (AnhCT), a catalytically inactive form of chymotrypsin, was shown to be effective for retaining active alpha-1-protease inhibitor (alpha-1-PI, also alpha-1-antitrypsin) from human plasma, while showing no measurable affinity for oxidized or protease complexed alpha-1-PI, or for most other plasma proteins. Sepharose 0-12 serpin family A member 1 Homo sapiens 306-316 6335631-5 1984 Therefore, an AnhCT-Sepharose 4B resin has been demonstrated to be of value for isolating active forms of alpha-1-PI from solutions, and may also be useful for the isolation of inter-alpha-trypsin inhibitor. Sepharose 20-29 serpin family A member 1 Homo sapiens 106-116 6600420-0 1983 Isoelectric focusing in agarose: classification of genetic variants of alpha 1-antitrypsin. Sepharose 24-31 serpin family A member 1 Homo sapiens 71-90 6600420-3 1983 We have developed a method for isoelectric focusing in agarose for the classification of alpha 1-antitrypsin variants. Sepharose 55-62 serpin family A member 1 Homo sapiens 89-108 6600421-6 1983 Furthermore the cigarette-smoke-damaged alpha 1-antitrypsin had an increased electrophoretic mobility in plain agarose compared with the pure protein and was more susceptible to proteolytic damage by elastase. Sepharose 111-118 serpin family A member 1 Homo sapiens 40-59 6983840-0 1982 An improved method for phenotyping of alpha 1-antitrypsin variants using separator isoelectric focusing on thin-layer agarose gel. Sepharose 118-125 serpin family A member 1 Homo sapiens 38-57 313929-1 1979 Two glycopeptides were obtained from alpha 1-protease inhibitor after extensive pronase digestion and chromatography on Bio-Gel P-10 and concanavalin A-Sepharose. Sepharose 152-161 serpin family A member 1 Homo sapiens 37-63 316999-4 1979 Affinity chromatography on heparin-Sepharose separated the proteins since alpha 1-AT did not bind to the matrix. Sepharose 35-44 serpin family A member 1 Homo sapiens 74-84 359714-0 1978 Quantitative immunofixation of proteins following zone electrophoresis in agarose gel: application to the determination of the stoichiometry of the alpha1-antitrypsin-elastase interaction. Sepharose 74-81 serpin family A member 1 Homo sapiens 148-166 312969-4 1979 Crossed antigen-antibody electrophoresis using agarose in both steps, immunoelectrophoresis, and agarose electrophoresis followed by immunofixation all revealed a slow-moving alpha1-antitrypsin, cathodal to the Pi Z region. Sepharose 97-104 serpin family A member 1 Homo sapiens 175-193 308033-1 1978 A group of 202 unrelated Italians were screened for alpha1-antitrypsin using agarose-acrylamide electrophoresis and isoelectric focusing. Sepharose 77-84 serpin family A member 1 Homo sapiens 52-70 383819-3 1979 Specificity of the antisera for A1AT was established by subsequent solid phase immunoadsorption against normal human serum bound to AH-Sepharose 4B. Sepharose 135-144 serpin family A member 1 Homo sapiens 32-36 1085169-1 1976 alpha 1-Antitrypsin phenotypes Pi M and Z, purified by the thiol-disulfide exchange procedure, were desialylated by treatment with neuraminidase covalently coupled to Sepharose and used as acceptors of sialic acid in an assay system for serum sialic acid transferase (CMP-N-acetylneuraminate:D-galactosyl-glycoprotein N-acetylneuraminyltransferase, EC 2.4.99.1) activity. Sepharose 167-176 serpin family A member 1 Homo sapiens 0-19 4198858-0 1973 [Separation of 2 forms of endobronchial alpha 1-antitrypsin using affinity chromatography on "Sepharose-trypsin"]. Sepharose 94-103 serpin family A member 1 Homo sapiens 40-59 32426967-3 2020 Serum protein A1AT was purified from patient sera by immunoprecipitation with anti-A1AT antibody conjugated agarose beads, and the isolated A1AT protein was digested and analyzed by LC-MS/MS. Sepharose 108-115 serpin family A member 1 Homo sapiens 14-18 403982-1 1977 The immunoprecipitation reaction for the determination of microamounts of alpha1-antitrypsin was conducted in the capillaries filled with a microvolume of a 1% agarose gel (the gel length was 7--8 mm, and the diameter--0.6 mm). Sepharose 160-167 serpin family A member 1 Homo sapiens 74-92 1087162-4 1976 Two additional products are identical to fragments of alpha-1-antitrypsin which can be washed from a column of Sepharose-bound elastase immediately after alpha-1-antitrypsin is applied to the column. Sepharose 111-120 serpin family A member 1 Homo sapiens 54-73 1081233-6 1975 In some peaks, only one or two protein bands are observed, suggesting that affinity chromatography on Sepharose- or Affi-Gel 10-chymotrypsin might be used for the isolation of alpha1-antitrypsin and other inhibitors in preparative amounts. Sepharose 102-111 serpin family A member 1 Homo sapiens 176-194 4603595-0 1974 [Identification of hereditary types of alpha-1-antitrypsin by acrylamide-agarose gel electrophoresis at pH 4.8]. Sepharose 73-80 serpin family A member 1 Homo sapiens 39-58 4542589-0 1973 Purification of human alpha 1-antitrypsin by affinity chromatography on sepharose bound concanavalin A. Sepharose 72-81 serpin family A member 1 Homo sapiens 22-41