PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1791469-0 1991 On the interaction of phosvitins with ferric ion: solubility of the Fe(III)-phosphoprotein complex under acidic conditions is a function of the iron/phosphate ratio and the degree of phosvitin phosphorylation. Iron 144-148 casein kinase 2 beta Homo sapiens 22-31 1791469-4 1991 At Fe/P ratios above 0.5, the Fe(III)-phosvitin complex becomes increasingly soluble. Iron 3-5 casein kinase 2 beta Homo sapiens 38-47 1791469-8 1991 The results imply that phosvitin iron binding sites are non-uniform and that, overall, phosvitin is capable of accommodating iron in different ways, depending on the relative magnitude of the iron load and the availability of phosphoserine clusters in the phosphoprotein. Iron 33-37 casein kinase 2 beta Homo sapiens 23-32 1791469-8 1991 The results imply that phosvitin iron binding sites are non-uniform and that, overall, phosvitin is capable of accommodating iron in different ways, depending on the relative magnitude of the iron load and the availability of phosphoserine clusters in the phosphoprotein. Iron 125-129 casein kinase 2 beta Homo sapiens 87-96 1791469-8 1991 The results imply that phosvitin iron binding sites are non-uniform and that, overall, phosvitin is capable of accommodating iron in different ways, depending on the relative magnitude of the iron load and the availability of phosphoserine clusters in the phosphoprotein. Iron 125-129 casein kinase 2 beta Homo sapiens 87-96 3822985-7 1986 Phosvitin demonstrated higher capacity to inhibit iron catalysis of phospholipid oxidations (up to 30:1 Fe2+-to-phosvitin molar ratio) than copper catalysis (1:1 molar ratio). Iron 50-54 casein kinase 2 beta Homo sapiens 0-9 35152755-5 2022 As a model system for a non-transparent food colloid such as mayonnaise, we designed an oil-in-water emulsion containing the ferric ion binding protein phosvitin commonly present in egg yolk. Iron 125-135 casein kinase 2 beta Homo sapiens 152-161 3822985-7 1986 Phosvitin demonstrated higher capacity to inhibit iron catalysis of phospholipid oxidations (up to 30:1 Fe2+-to-phosvitin molar ratio) than copper catalysis (1:1 molar ratio). Iron 50-54 casein kinase 2 beta Homo sapiens 112-121 3822985-8 1986 Pasteurization did not change the antioxidant activities of phosvitin; however, autoclaving decreased phosvitin"s inhibitory capacity on iron catalysis. Iron 137-141 casein kinase 2 beta Homo sapiens 102-111 28485214-1 2017 The flavor deterioration of mayonnaise is induced by iron, which is released from egg yolk phosvitin under acidic conditions and promotes lipid oxidation. Iron 53-57 casein kinase 2 beta Homo sapiens 91-100 13980103-0 1963 Interaction between phosvitin and iron and its effect on a rearrangement of phosvitin structure. Iron 34-38 casein kinase 2 beta Homo sapiens 20-29 13980103-0 1963 Interaction between phosvitin and iron and its effect on a rearrangement of phosvitin structure. Iron 34-38 casein kinase 2 beta Homo sapiens 76-85 31206850-3 2019 Phosvitin was chosen as a relevant model for phosphorylated proteins because of its important role as an iron, calcium, and magnesium storage protein in egg yolk. Iron 105-109 casein kinase 2 beta Homo sapiens 0-9 30474149-0 2019 31 P NMR assessment of the phosvitin-iron complex in mayonnaise. Iron 37-41 casein kinase 2 beta Homo sapiens 27-36 30474149-2 2019 One of the main catalysts of this process is iron, which is introduced in its ferric (Fe(III)) form via phosvitin, an egg yolk phosphoprotein rich in phosphoserines. Iron 45-49 casein kinase 2 beta Homo sapiens 104-113 3711888-0 1986 Iron binding by phosvitin: variation of rate of iron release as a function of the degree of saturation of iron binding sites. Iron 0-4 casein kinase 2 beta Homo sapiens 16-25 3711888-0 1986 Iron binding by phosvitin: variation of rate of iron release as a function of the degree of saturation of iron binding sites. Iron 48-52 casein kinase 2 beta Homo sapiens 16-25 3711888-0 1986 Iron binding by phosvitin: variation of rate of iron release as a function of the degree of saturation of iron binding sites. Iron 106-110 casein kinase 2 beta Homo sapiens 16-25 3711888-1 1986 The rate of iron release from Fe(III)-phosvitin complexes, at varied degrees of saturation, was studied. Iron 12-16 casein kinase 2 beta Homo sapiens 38-47 3006970-4 1986 The study reported here focuses on the effects of phosvitin, a suspected inhibitor of iron absorption found in egg yolks, on the chemistry of iron during the in vitro enzymatic digestion of pinto beans. Iron 86-90 casein kinase 2 beta Homo sapiens 50-59 3006970-4 1986 The study reported here focuses on the effects of phosvitin, a suspected inhibitor of iron absorption found in egg yolks, on the chemistry of iron during the in vitro enzymatic digestion of pinto beans. Iron 142-146 casein kinase 2 beta Homo sapiens 50-59 7188938-0 1980 Iron binding by phosvitin and its conformational consequences. Iron 0-4 casein kinase 2 beta Homo sapiens 16-25 7188938-1 1980 With a view to the potential biological significance of iron binding by the phosphoprotein phosvitin, the interaction of these two electrostatically complementary constituents of egg yolk particles was studied by ultrafiltration, circular dichroism, and sedimentation. Iron 56-60 casein kinase 2 beta Homo sapiens 91-100 7188938-3 1980 When saturated, pairs of the approximately 135 phosphate groups of a phosvitin molecule appear to bind 1 iron atom each. Iron 105-109 casein kinase 2 beta Homo sapiens 69-78 7188938-8 1980 Nevertheless, iron affects phosvitin structure. Iron 14-18 casein kinase 2 beta Homo sapiens 27-36 7188938-10 1980 Near pH 2, where the beta-type conformation is readily acquired by the protein in the absence of iron, the consequences of iron binding upon conformation are determined by the manner in which the iron-phosvitin interaction is brought about. Iron 97-101 casein kinase 2 beta Homo sapiens 201-210 7188938-10 1980 Near pH 2, where the beta-type conformation is readily acquired by the protein in the absence of iron, the consequences of iron binding upon conformation are determined by the manner in which the iron-phosvitin interaction is brought about. Iron 123-127 casein kinase 2 beta Homo sapiens 201-210 7188938-10 1980 Near pH 2, where the beta-type conformation is readily acquired by the protein in the absence of iron, the consequences of iron binding upon conformation are determined by the manner in which the iron-phosvitin interaction is brought about. Iron 123-127 casein kinase 2 beta Homo sapiens 201-210 975400-1 1976 It has been suggested that the binding of iron(III) by phosvitin involves the phosphoric radicals of phosphorylserine residues, many of which are arranged in rows of several consecutive phosphoamino acids. Iron 42-46 casein kinase 2 beta Homo sapiens 55-64 975400-4 1976 These findings indicate that polyphosphorylserine blocks play an important role in the binding of iron by phosvitin, and that in the intact protein their binding capacity is optimized by the conformation of the polypeptide chain. Iron 98-102 casein kinase 2 beta Homo sapiens 106-115 32966601-5 2020 Phosvitin, which has many functional features thanks to its unique structure, is known primarily for its metal bonds binding (iron, calcium, etc.) Iron 126-130 casein kinase 2 beta Homo sapiens 0-9 32966601-8 2020 Although this feature of phosvitin may partially decrease the bioavailability of especially iron in the egg, it allows the phosvitin to have many bioactivities in the food industry and health. Iron 92-96 casein kinase 2 beta Homo sapiens 25-34 32966601-9 2020 Lipid oxidation, which is a serious problem in the food industry, can be inhibited by adding phosvitin and its derived phosphopeptides to the food production chain via inhibiting bivalent iron. Iron 188-192 casein kinase 2 beta Homo sapiens 93-102 25049750-3 2013 The optimal pH for the phosvitin extraction from yolk granules was determined, and the iron-binding ability of the extracted phosvitin (final product) was tested. Iron 87-91 casein kinase 2 beta Homo sapiens 125-134 15215598-1 2004 Phosvitin, a phosphoprotein known as an iron-carrier in egg yolk, binds almost all the yolk iron. Iron 40-44 casein kinase 2 beta Homo sapiens 0-9 15215598-4 2004 The effectiveness of phosvitin was related to the iron concentration, indicating that phosvitin acts as an antioxidant by chelating iron ions. Iron 50-54 casein kinase 2 beta Homo sapiens 86-95 15215598-4 2004 The effectiveness of phosvitin was related to the iron concentration, indicating that phosvitin acts as an antioxidant by chelating iron ions. Iron 132-136 casein kinase 2 beta Homo sapiens 21-30 15215598-4 2004 The effectiveness of phosvitin was related to the iron concentration, indicating that phosvitin acts as an antioxidant by chelating iron ions. Iron 132-136 casein kinase 2 beta Homo sapiens 86-95 15215598-1 2004 Phosvitin, a phosphoprotein known as an iron-carrier in egg yolk, binds almost all the yolk iron. Iron 92-96 casein kinase 2 beta Homo sapiens 0-9 15215598-3 2004 Using electron spin resonance (ESR) with 5,5-dimethyl-1-pyrroline-N-oxide (DMPO) and deoxyribose degradation assays, we observed by both assays that phosvitin more effectively inhibited (.-)OH formation than iron-binding proteins such as ferritin and transferrin. Iron 208-212 casein kinase 2 beta Homo sapiens 149-158 15215598-4 2004 The effectiveness of phosvitin was related to the iron concentration, indicating that phosvitin acts as an antioxidant by chelating iron ions. Iron 50-54 casein kinase 2 beta Homo sapiens 21-30