PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2813359-6 1989 From examination of various preparations of recombinant human EPO, we found a positive correlation between the in vivo activity of EPO and the ratio of tetraantennary to biantennary oligosaccharides. Oligosaccharides 182-198 erythropoietin Homo sapiens 62-65 2813359-6 1989 From examination of various preparations of recombinant human EPO, we found a positive correlation between the in vivo activity of EPO and the ratio of tetraantennary to biantennary oligosaccharides. Oligosaccharides 182-198 erythropoietin Homo sapiens 131-134 2550193-4 1989 Oligosaccharide structure analyses suggested that almost all N-linked oligosaccharide chains of Namalwa EPO are shared by urinary EPO. Oligosaccharides 0-15 erythropoietin Homo sapiens 104-107 2960381-7 1987 This difference was attributed to the glycosylation of erythropoietin in S. frugiperda cells with oligosaccharides of only limited size. Oligosaccharides 98-114 erythropoietin Homo sapiens 55-69 2752139-6 1989 Chemically, this erythropoietin (molecular weight [mol wt] 26,200) appears exceptionally uniform in its oligosaccharide constitution (30%) as contrasted with heterogeneously glycosylated erythropoietins derived from mammalian cells (mol wt 30,000 to 38,000; 40% to 50% complex-type oligosaccharide). Oligosaccharides 104-119 erythropoietin Homo sapiens 17-31 2752139-6 1989 Chemically, this erythropoietin (molecular weight [mol wt] 26,200) appears exceptionally uniform in its oligosaccharide constitution (30%) as contrasted with heterogeneously glycosylated erythropoietins derived from mammalian cells (mol wt 30,000 to 38,000; 40% to 50% complex-type oligosaccharide). Oligosaccharides 282-297 erythropoietin Homo sapiens 17-31 3179269-4 1988 More than 8 and 13 kinds of oligosaccharide fractions for u-EPO and r-EPO (BHK), respectively, were completely separated by the one-step HPLC procedure. Oligosaccharides 28-43 erythropoietin Homo sapiens 60-63 3179269-4 1988 More than 8 and 13 kinds of oligosaccharide fractions for u-EPO and r-EPO (BHK), respectively, were completely separated by the one-step HPLC procedure. Oligosaccharides 28-43 erythropoietin Homo sapiens 70-73 3996312-8 1985 Limited proteolysis of [3H]epo (labeled at sialic acid residues of the oligosaccharide chains) showed that it consists of two rather trypsin-resistant domains, each having a mol wt of about 16,000, connected by a small region of protein that is trypsin sensitive. Oligosaccharides 71-86 erythropoietin Homo sapiens 27-30 3996313-5 1985 These findings indicate that the oligosaccharide portion of epo, although required for action in vivo, is not required for interaction with the target cells of the blood-forming system. Oligosaccharides 33-48 erythropoietin Homo sapiens 60-63 22180204-5 2011 Furthermore, we applied the proposed method for the analyses of N-linked sialo- and asialo-oligosaccharides in glycoproteins (ribonuclease B, fetuin, and recombinant human erythropoietin). Oligosaccharides 91-107 erythropoietin Homo sapiens 172-186 30774876-4 2019 Insights obtained from attempted folding of our "click" neoglycoprotein EPO analogue, bearing four different neutral sugar moieties, highlight the important role played by the charged oligosaccharides present in native EPO glycoproteins. Oligosaccharides 184-200 erythropoietin Homo sapiens 72-75 30774876-4 2019 Insights obtained from attempted folding of our "click" neoglycoprotein EPO analogue, bearing four different neutral sugar moieties, highlight the important role played by the charged oligosaccharides present in native EPO glycoproteins. Oligosaccharides 184-200 erythropoietin Homo sapiens 219-222 16937399-2 2007 For glycoproteins, such as erythropoietin (EPO), posttranslational processing involves the addition of oligosaccharide chains. Oligosaccharides 103-118 erythropoietin Homo sapiens 27-41 20349507-6 2010 This review describes recent progress related to the efficient method of oligosaccharide preparation and synthesis of glycoproteins including bioactive erythropoietin. Oligosaccharides 73-88 erythropoietin Homo sapiens 152-166 19653112-2 2010 The recombinant hEpo was produced in the serum and egg white of the GM chickens, and the oligosaccharide chain structures of the serum-derived hEpo were more favorable than those of the egg white-derived hEpo. Oligosaccharides 89-104 erythropoietin Homo sapiens 16-20 19653112-2 2010 The recombinant hEpo was produced in the serum and egg white of the GM chickens, and the oligosaccharide chain structures of the serum-derived hEpo were more favorable than those of the egg white-derived hEpo. Oligosaccharides 89-104 erythropoietin Homo sapiens 143-147 19653112-2 2010 The recombinant hEpo was produced in the serum and egg white of the GM chickens, and the oligosaccharide chain structures of the serum-derived hEpo were more favorable than those of the egg white-derived hEpo. Oligosaccharides 89-104 erythropoietin Homo sapiens 143-147 19653112-5 2010 Lectin blot analyses revealed that significant amounts of the oligosaccharide chains of hEpo/Fc produced in the serum and eggs of GM chickens terminated with galactose, and that the oligosaccharide chains of the serum- and yolk-derived hEpo/Fc incorporated sialic acid residues. Oligosaccharides 62-77 erythropoietin Homo sapiens 88-92 20550136-7 2010 Human erythropoietin (hEPO) bearing highly sialylated oligosaccharide was shown to display a much longer plasma half-life, resulting in high therapeutic efficacy. Oligosaccharides 54-69 erythropoietin Homo sapiens 6-20 19334683-1 2009 Single erythropoietin (EPO) glycoforms with defined mature oligosaccharide structures and amino acid sequences are essential to elucidate the molecular mechanisms by which carbohydrates exert various physiological and metabolic functions and to explore the possible links between carbohydrates and the prevention or management of diseases. Oligosaccharides 59-74 erythropoietin Homo sapiens 7-21 19334683-1 2009 Single erythropoietin (EPO) glycoforms with defined mature oligosaccharide structures and amino acid sequences are essential to elucidate the molecular mechanisms by which carbohydrates exert various physiological and metabolic functions and to explore the possible links between carbohydrates and the prevention or management of diseases. Oligosaccharides 59-74 erythropoietin Homo sapiens 23-26 16937399-2 2007 For glycoproteins, such as erythropoietin (EPO), posttranslational processing involves the addition of oligosaccharide chains. Oligosaccharides 103-118 erythropoietin Homo sapiens 43-46 14628453-4 2003 Oligosaccharides were labeled with a sensitive fluorescent dye 8-aminopyrene-1,3,6-trisulfonate (APTS), and all of the labeled oligosaccharides released from EPO were mapped by capillary gel electrophoresis with laser-induced fluorescence. Oligosaccharides 127-143 erythropoietin Homo sapiens 158-161 16475009-0 2006 Dynamic control of oligosaccharide modification in the mammary gland: linking recombinant human erythropoietin functional analysis of transgenic mouse milk-derived hEPO. Oligosaccharides 19-34 erythropoietin Homo sapiens 164-168 14628453-10 2003 In case of asialyated N-glycan mapping, the retention time of each oligosaccharide delayed greatly, and most importantly, the resulted sialic acid peak can be used as a quantitative standard to determine sialic acid content in N-glycans of EPO. Oligosaccharides 67-82 erythropoietin Homo sapiens 240-243 9350435-10 1997 The role of oligosaccharides in EPO may be to protect the protein structure from active oxygen radicals. Oligosaccharides 12-28 erythropoietin Homo sapiens 32-35 10998266-3 2000 Many different sialylated oligosaccharides of EPO were separated and characterized by LC/MS equipped with a graphitized carbon column (GCC). Oligosaccharides 26-42 erythropoietin Homo sapiens 46-49 9402140-2 1997 Epo is a glycoprotein with a molecular mass of approx 30 kDa, which circulates in plasma of the human with 165 amino acids with three N-linked and one O-linked acidic oligosaccharide side chains in the molecule. Oligosaccharides 167-182 erythropoietin Homo sapiens 0-3 12691916-2 2003 This led to the hypothesis that an EPO analogue engineered to contain additional oligosaccharide chains would have enhanced biological activity. Oligosaccharides 81-96 erythropoietin Homo sapiens 35-38 11739166-8 2001 Determination of charge state after treatment of human serum EPO with Arthrobacter ureafaciens sialidase showed that the acidity of the oligosaccharide structures was caused by sialic acids. Oligosaccharides 136-151 erythropoietin Homo sapiens 61-64 11027166-14 2000 In conclusion, we showed that ammonia in the culture medium affected EPO glycosylation, which was observed as a reduction of the tetraantennary and tetrasialylated oligosaccharide structures. Oligosaccharides 164-179 erythropoietin Homo sapiens 69-72 9823711-8 1998 In this study, oligosaccharides derived from the enzymatic cleavage of the sugar chains of glycoproteins ribonuclease B, erythropoietin, and transferrin were subjected to ABDEAE derivatization, prior to analysis on a matrix-assisted laser desorption/ionization time-of-flight mass spectrometer (MALDI-TOF MS) for high-resolution mass measurement and a postsource decay (PSD) experiment. Oligosaccharides 15-31 erythropoietin Homo sapiens 121-135 7781780-1 1995 A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site. Oligosaccharides 220-235 erythropoietin Homo sapiens 113-127 7764406-0 1994 Automated analysis of the oligosaccharides from recombinant erythropoietin. Oligosaccharides 26-42 erythropoietin Homo sapiens 60-74 8054720-0 1994 Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Oligosaccharides 55-70 erythropoietin Homo sapiens 99-113 8477709-0 1993 Structures of sialylated oligosaccharides of human erythropoietin expressed in recombinant BHK-21 cells. Oligosaccharides 25-41 erythropoietin Homo sapiens 51-65 8444888-7 1993 This recombinant erythropoietin was found to contain eight times more tetrasialylated oligosaccharides than previously reported (Sasaki, H., Bothner, B., Dell, A., and Fukuda, M. (1987) J. Biol. Oligosaccharides 86-102 erythropoietin Homo sapiens 17-31 8460945-4 1993 All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc. Oligosaccharides 73-89 erythropoietin Homo sapiens 48-62