PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7436742-1 1980 Lipoprotein lipase of bovine aortic intima has been purified to homogeneity by affinity chromatography on heparin-Sepharose. Sepharose 114-123 lipoprotein lipase Bos taurus 0-18 826537-2 1976 Lipoprotein lipase of high purity has been isolated from bovine milk by affinity chromatography on heparin-Sepharose, adsorption to Cgamma-aluminum hydroxide gel, and intervent dilution chromatography on heparin-Sepharose. Sepharose 107-116 lipoprotein lipase Bos taurus 0-18 563231-0 1977 Interaction of lipoprotein lipase with heparin-Sepharose. Sepharose 47-56 lipoprotein lipase Bos taurus 15-33 826537-2 1976 Lipoprotein lipase of high purity has been isolated from bovine milk by affinity chromatography on heparin-Sepharose, adsorption to Cgamma-aluminum hydroxide gel, and intervent dilution chromatography on heparin-Sepharose. Sepharose 212-221 lipoprotein lipase Bos taurus 0-18 1009091-1 1976 Lipoprotein lipase has been purified from bovine milk by affinity chromatography on Sepharose containing covalently linked heparin. Sepharose 84-93 lipoprotein lipase Bos taurus 0-18 1654330-3 1991 To identify this LPL binding protein(s), radioiodinated cell surface proteins from cultured bovine aortic endothelial cells were chromatographed using bovine LPL-Sepharose. Sepharose 162-171 lipoprotein lipase Bos taurus 17-20 4633808-0 1973 Validation of a "clearing" assay for milk lipoprotein lipase in agarose gel. Sepharose 64-71 lipoprotein lipase Bos taurus 42-60 4633808-1 1973 We have developed a simplified method for the quantitative assay of lipoprotein lipase in cow"s milk based on the hydrolysis of a glyceride emulsion in semisolid agarose gel. Sepharose 162-169 lipoprotein lipase Bos taurus 68-86 9480888-3 1998 In order to investigate this, we isolated LPL from bovine milk via heparin Sepharose chromatography using a continuous salt gradient. Sepharose 75-84 lipoprotein lipase Bos taurus 42-45 9548595-11 1998 Heparin-Sepharose chromatography of wild-type LPL and a mutant LPL in which the well-characterized heparin-binding sequence (Arg 281-Lys 282-Arg 284) has been mutated was carried out in the presence and absence of xCAL 3-6a. Sepharose 8-17 lipoprotein lipase Bos taurus 46-49 9548595-11 1998 Heparin-Sepharose chromatography of wild-type LPL and a mutant LPL in which the well-characterized heparin-binding sequence (Arg 281-Lys 282-Arg 284) has been mutated was carried out in the presence and absence of xCAL 3-6a. Sepharose 8-17 lipoprotein lipase Bos taurus 63-66 1654330-3 1991 To identify this LPL binding protein(s), radioiodinated cell surface proteins from cultured bovine aortic endothelial cells were chromatographed using bovine LPL-Sepharose. Sepharose 162-171 lipoprotein lipase Bos taurus 158-161 1654330-7 1991 A 220-kDa protein from the basal cell surface was also identified using LPL-Sepharose chromatography. Sepharose 76-85 lipoprotein lipase Bos taurus 72-75 2015950-2 1991 A triglyceride (TG) lipase is present in whole homogenate and tissue extracts of beef myocardium with characteristics of lipoprotein lipase (LPL); i.e., activity is stimulated by serum, inhibited by NaCl and protamine sulfate, the protein binds to heparin-Sepharose, and the enzyme has an alkaline pH optimum. Sepharose 256-265 lipoprotein lipase Bos taurus 121-139 2015950-2 1991 A triglyceride (TG) lipase is present in whole homogenate and tissue extracts of beef myocardium with characteristics of lipoprotein lipase (LPL); i.e., activity is stimulated by serum, inhibited by NaCl and protamine sulfate, the protein binds to heparin-Sepharose, and the enzyme has an alkaline pH optimum. Sepharose 256-265 lipoprotein lipase Bos taurus 141-144 2222404-3 1990 The lipase bound to heparin-agarose and co-eluted with 125I-labelled bovine lipoprotein lipase in a salt gradient. Sepharose 28-35 lipoprotein lipase Bos taurus 76-94 2317527-8 1990 Release of LPL from heparin-agarose followed a similar pattern, suggesting that the fatty acids specifically affected LPL-heparin interaction. Sepharose 28-35 lipoprotein lipase Bos taurus 11-14 2317527-11 1990 Only the prior incubation with LPL affected the binding to heparin-agarose. Sepharose 67-74 lipoprotein lipase Bos taurus 31-34 2300584-8 1990 Model studies with bovine LPL showed that fatty acids displace the enzyme from heparin-agarose. Sepharose 87-94 lipoprotein lipase Bos taurus 26-29 2581953-2 1985 Lipoprotein lipase was purified from bovine skim milk by chromatography on heparin-Sepharose. Sepharose 83-92 lipoprotein lipase Bos taurus 0-18 2581953-6 1985 Incubation of partially purified lipoprotein lipase for 24 h at 37 degrees C results in breakdown of the 55,000-dalton protein with concomitant enrichment in lower Mr components; the proteolytic activity is prevented by incubating the milk with phenylmethane, sulfonyl fluoride prior to chromatography on heparin-Sepharose. Sepharose 313-322 lipoprotein lipase Bos taurus 33-51 4059181-1 1985 Lipoprotein lipase was purified to homogeneity from bovine skim milk by a two-step procedure using chromatography on heparin-Sepharose. Sepharose 125-134 lipoprotein lipase Bos taurus 0-18 6639055-0 1983 The comparative kinetics of soluble and heparin-Sepharose-immobilized bovine lipoprotein lipase. Sepharose 48-57 lipoprotein lipase Bos taurus 77-95 6639055-2 1983 Hence kinetic parameters of S-LPL and heparin-Sepharose-immobilized LPL (B-LPL) were compared. Sepharose 46-55 lipoprotein lipase Bos taurus 68-71 6639055-2 1983 Hence kinetic parameters of S-LPL and heparin-Sepharose-immobilized LPL (B-LPL) were compared. Sepharose 46-55 lipoprotein lipase Bos taurus 73-78 6639055-10 1983 It is concluded that most of the LPL bound to heparin-Sepharose is probably inaccessible to substrate, hence a low Vmax. Sepharose 54-63 lipoprotein lipase Bos taurus 33-36 7159570-3 1982 The same protein and same active site are involved in hydrolysis of water-soluble p-nitrophenyl esters and emulsified trioleoylglycerol since (a) trioleoylglycerol hydrolysis and PNPB hydrolysis activities coelute from the heparin-Sepharose affinity column used to purify LpL and (b) LpL-catalyzed hydrolyses of trioleoylglycerol and PNPB are inhibited to equal extents by phenylmethanesulfonyl fluoride. Sepharose 231-240 lipoprotein lipase Bos taurus 272-275 7159570-3 1982 The same protein and same active site are involved in hydrolysis of water-soluble p-nitrophenyl esters and emulsified trioleoylglycerol since (a) trioleoylglycerol hydrolysis and PNPB hydrolysis activities coelute from the heparin-Sepharose affinity column used to purify LpL and (b) LpL-catalyzed hydrolyses of trioleoylglycerol and PNPB are inhibited to equal extents by phenylmethanesulfonyl fluoride. Sepharose 231-240 lipoprotein lipase Bos taurus 284-287