PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20455239-3 2010 Selective oxidation of the sialic acid residues on the glycan chains of transferrin was followed by introduction of a terminal alkyne functionality through an oxime linkage. N-Acetylneuraminic Acid 27-38 transferrin Homo sapiens 72-83 18006263-3 2008 These results provide strong evidence that the sialic acid residue in TF masks its binding ability to serum proteins. N-Acetylneuraminic Acid 47-58 transferrin Homo sapiens 70-72 19281805-7 2009 Monitoring the pattern of transferrin bound sialic acid residues may thus be a helpful tool in assessing the risk of malignant degeneration in patients with chronic fibrogenic liver disease. N-Acetylneuraminic Acid 44-55 transferrin Homo sapiens 26-37 19153153-5 2009 Two-dimensional gel analyses revealed significant hyposialylation of transferrin in CSF of all patients compared to age-matched controls (P < 0.001)--a finding not present in the CSF of patients with Salla disease, the most common free sialic acid storage disorder. N-Acetylneuraminic Acid 239-250 transferrin Homo sapiens 69-80 14760639-1 2004 Carbohydrate-deficient transferrin (CDT) is the most specific marker for diagnosis of chronic excessive alcohol consumption and includes the serum transferrin (Tf) isoforms with two or less sialic acid residues (di-, mono-, and asialo-Tf). N-Acetylneuraminic Acid 190-201 transferrin Homo sapiens 23-34 16041604-9 2005 This hybrid technique proved more selective and reliable detection of transferrin isoforms with 2, 3, 4, 5, and 6 sialic acid residues (S(2), S(3), S(4), S(5), and S(6)) in real serum samples. N-Acetylneuraminic Acid 114-125 transferrin Homo sapiens 70-81 15988320-3 2005 Human serum transferrin contains two biantennary glycans, each consisting of 0 to 4 molecules of sialic acid (SA); its SA content is heterogeneous with high concentration of tetrasialotransferrin (4SA) and low amounts of disialo-, trisialo-, penta-, and hexasialotransferrin. N-Acetylneuraminic Acid 97-108 transferrin Homo sapiens 12-23 15988320-3 2005 Human serum transferrin contains two biantennary glycans, each consisting of 0 to 4 molecules of sialic acid (SA); its SA content is heterogeneous with high concentration of tetrasialotransferrin (4SA) and low amounts of disialo-, trisialo-, penta-, and hexasialotransferrin. N-Acetylneuraminic Acid 110-112 transferrin Homo sapiens 12-23 15988320-3 2005 Human serum transferrin contains two biantennary glycans, each consisting of 0 to 4 molecules of sialic acid (SA); its SA content is heterogeneous with high concentration of tetrasialotransferrin (4SA) and low amounts of disialo-, trisialo-, penta-, and hexasialotransferrin. N-Acetylneuraminic Acid 119-121 transferrin Homo sapiens 12-23 15988320-11 2005 In a sheep model of septic shock secondary to peritonitis, serum free SA was already increased after 15 h. Sepsis is associated with decreased SA content on circulating transferrin and with an increase in blood free SA concentrations. N-Acetylneuraminic Acid 143-145 transferrin Homo sapiens 169-180 15988320-11 2005 In a sheep model of septic shock secondary to peritonitis, serum free SA was already increased after 15 h. Sepsis is associated with decreased SA content on circulating transferrin and with an increase in blood free SA concentrations. N-Acetylneuraminic Acid 143-145 transferrin Homo sapiens 169-180 17165810-2 2006 However, CDT is not a single molecular entity but refers to a group of sialic acid-deficient transferrin isoforms from mono- to trisialotransferrin. N-Acetylneuraminic Acid 71-82 transferrin Homo sapiens 93-104 16538641-1 2006 Sialic acid (SA) is responsible for the composition of different isoforms of transferrin and is reported to be a marker of microvascular complications in type 2 diabetes mellitus. N-Acetylneuraminic Acid 0-11 transferrin Homo sapiens 77-88 16538641-1 2006 Sialic acid (SA) is responsible for the composition of different isoforms of transferrin and is reported to be a marker of microvascular complications in type 2 diabetes mellitus. N-Acetylneuraminic Acid 13-15 transferrin Homo sapiens 77-88 14760639-1 2004 Carbohydrate-deficient transferrin (CDT) is the most specific marker for diagnosis of chronic excessive alcohol consumption and includes the serum transferrin (Tf) isoforms with two or less sialic acid residues (di-, mono-, and asialo-Tf). N-Acetylneuraminic Acid 190-201 transferrin Homo sapiens 147-158 14760639-1 2004 Carbohydrate-deficient transferrin (CDT) is the most specific marker for diagnosis of chronic excessive alcohol consumption and includes the serum transferrin (Tf) isoforms with two or less sialic acid residues (di-, mono-, and asialo-Tf). N-Acetylneuraminic Acid 190-201 transferrin Homo sapiens 160-162 14604115-8 2003 Tf patterns are recognized and identified via detection times of Tf isoforms (intra-day and inter-day RSD values < 1.0% and < 1.7%, respectively), immunosubtraction of Tf and enzymatic sequential cleavage of sialic acid residues. N-Acetylneuraminic Acid 214-225 transferrin Homo sapiens 0-2 11689212-9 2001 Serum trans-sialidase transferred sialic acid from glycoconjugates of plasma proteins (fetuin, transferrin) and gangliosides (GM3, GD3, GM1, GD1a, GD1b). N-Acetylneuraminic Acid 34-45 transferrin Homo sapiens 95-106 11325539-0 2001 Effects of sialic acid residues of transferrin on the binding with aluminum and iron studied by HPLC/high-resolution ICP-MS. Transferrins (Tfs) are glycoproteins with carbohydrate chains in the C-lobe. N-Acetylneuraminic Acid 11-22 transferrin Homo sapiens 35-46 10963781-2 2000 The main component of normal serum transferrin contains two biantennary glycans, each consisting of 2 mol of sialic acid (Tetrasialo transferrin). N-Acetylneuraminic Acid 109-120 transferrin Homo sapiens 35-46 10963781-2 2000 The main component of normal serum transferrin contains two biantennary glycans, each consisting of 2 mol of sialic acid (Tetrasialo transferrin). N-Acetylneuraminic Acid 109-120 transferrin Homo sapiens 133-144 10939448-1 2000 Transferrin, an iron transport protein found in serum and cerebrospinal fluid, is known to be microheterogeneous with respect to its carbohydrate and sialic acid content. N-Acetylneuraminic Acid 150-161 transferrin Homo sapiens 0-11 10939448-2 2000 The forms of transferrin deficient in sialic acid and/or carbohydrate, termed carbohydrate-deficient transferrin (CDT), have been of clinical interest for almost two decades as a result of the initial finding that elevated CDT concentrations are associated with chronic, excessive alcohol abuse. N-Acetylneuraminic Acid 38-49 transferrin Homo sapiens 13-24 10939448-2 2000 The forms of transferrin deficient in sialic acid and/or carbohydrate, termed carbohydrate-deficient transferrin (CDT), have been of clinical interest for almost two decades as a result of the initial finding that elevated CDT concentrations are associated with chronic, excessive alcohol abuse. N-Acetylneuraminic Acid 38-49 transferrin Homo sapiens 101-112 10892586-1 2000 Transferrin sialoforms with fewer than three sialic acid residues (carbohydrate deficient transferrin; CDT) have been implicated as a marker of certain liver pathologies. N-Acetylneuraminic Acid 45-56 transferrin Homo sapiens 0-11 9516657-6 1998 Isoforms lacking one to eight of four to eight possible sialic acid residues were found in AT, TBG and Tf in all cases, with variable intensity and frequency, and in all except one patient in alpha(1)-AT. N-Acetylneuraminic Acid 56-67 transferrin Homo sapiens 103-105 10217151-1 1999 It is well-known that microheterogeneity of human serum transferrin observed in alcoholics manifests as sialic acid-deficient transferrin isoforms, otherwise known as carbohydrate-deficient transferrin (CDT). N-Acetylneuraminic Acid 104-115 transferrin Homo sapiens 56-67 10217151-1 1999 It is well-known that microheterogeneity of human serum transferrin observed in alcoholics manifests as sialic acid-deficient transferrin isoforms, otherwise known as carbohydrate-deficient transferrin (CDT). N-Acetylneuraminic Acid 104-115 transferrin Homo sapiens 126-137 10217151-1 1999 It is well-known that microheterogeneity of human serum transferrin observed in alcoholics manifests as sialic acid-deficient transferrin isoforms, otherwise known as carbohydrate-deficient transferrin (CDT). N-Acetylneuraminic Acid 104-115 transferrin Homo sapiens 126-137 9870409-2 1998 It consists of a group of minor isoforms of human transferrin (the main iron transport serum protein) deficient in sialic acid groups (asialo, monosialo and disialo) with a pI > 5.7, while the main isotransferrin (tetrasialo) has a pI of 5.4. N-Acetylneuraminic Acid 115-126 transferrin Homo sapiens 50-61 10763998-14 2000 Neuraminidase was used to digest sialic acid side chains from pure transferrin in solution, and the reaction product was used as a reference standard for comparison to assay of unknown fluids. N-Acetylneuraminic Acid 33-44 transferrin Homo sapiens 67-78 10744316-2 2000 It indicates a group of isoforms of human transferrin (Tf), the main iron transport serum protein, deficient in sialic acid residues (asialo-, monosialo- and disialo-Tf) in comparison to the main isotransferrin which contains four sialic acid groups (tetrasialo-Tf). N-Acetylneuraminic Acid 112-123 transferrin Homo sapiens 42-53 10744316-2 2000 It indicates a group of isoforms of human transferrin (Tf), the main iron transport serum protein, deficient in sialic acid residues (asialo-, monosialo- and disialo-Tf) in comparison to the main isotransferrin which contains four sialic acid groups (tetrasialo-Tf). N-Acetylneuraminic Acid 112-123 transferrin Homo sapiens 55-57 10744316-2 2000 It indicates a group of isoforms of human transferrin (Tf), the main iron transport serum protein, deficient in sialic acid residues (asialo-, monosialo- and disialo-Tf) in comparison to the main isotransferrin which contains four sialic acid groups (tetrasialo-Tf). N-Acetylneuraminic Acid 231-242 transferrin Homo sapiens 42-53 10744316-2 2000 It indicates a group of isoforms of human transferrin (Tf), the main iron transport serum protein, deficient in sialic acid residues (asialo-, monosialo- and disialo-Tf) in comparison to the main isotransferrin which contains four sialic acid groups (tetrasialo-Tf). N-Acetylneuraminic Acid 231-242 transferrin Homo sapiens 55-57 10571009-3 1999 Due to the deficiency of terminal N-acetylneuraminic acid or sialic acid, the glycan changes can be observed in serum transferrin or other glycoproteins using isoelectrofocusing with immunofixation as the most widely used diagnostic technique. N-Acetylneuraminic Acid 34-57 transferrin Homo sapiens 118-129 10571009-3 1999 Due to the deficiency of terminal N-acetylneuraminic acid or sialic acid, the glycan changes can be observed in serum transferrin or other glycoproteins using isoelectrofocusing with immunofixation as the most widely used diagnostic technique. N-Acetylneuraminic Acid 61-72 transferrin Homo sapiens 118-129 8605672-3 1996 Sialic acid-deficient transferrin fractions are collected in the eluate, and transferrin is then quantified by a rate-nephelometric technique. N-Acetylneuraminic Acid 0-11 transferrin Homo sapiens 22-33 7503419-7 1995 In conclusion, inappropriate isoelectric focusing conditions strongly affect iron load stability of isotransferrins (obviously via low pH within the gel), resulting in transferrin iron release and cofocusing of isotransferrins with different sialic acid or iron contents. N-Acetylneuraminic Acid 242-253 transferrin Homo sapiens 103-114 7652979-1 1995 Carbohydrate deficient transferrin (CDT) is an isoform of transferrin with a reduced carbohydrate content, especially the negatively charged sialic acid. N-Acetylneuraminic Acid 141-152 transferrin Homo sapiens 23-34 7652979-1 1995 Carbohydrate deficient transferrin (CDT) is an isoform of transferrin with a reduced carbohydrate content, especially the negatively charged sialic acid. N-Acetylneuraminic Acid 141-152 transferrin Homo sapiens 58-69 2592487-3 1989 The pattern changed when iron-free transferrin was treated with neuraminidase, which splits off the sialic acid from the carbohydrate chains. N-Acetylneuraminic Acid 100-111 transferrin Homo sapiens 35-46 8138529-6 1993 Transferrin isoforms containing 4, 2, and 0 sialic acid residues, S4, S2, and S0, were separated by Mono Q anion exchange column chromatography from serum of a patient with the CDG syndrome. N-Acetylneuraminic Acid 44-55 transferrin Homo sapiens 0-11 8286854-5 1993 The deficiency of sialic acid, in particular, results in a cathodal shift and hence the presence of abnormal isoforms of transferrin with higher isoelectric points than normal. N-Acetylneuraminic Acid 18-29 transferrin Homo sapiens 121-132 1443784-2 1992 The abnormal transferrin contains reduced amounts of carbohydrates, especially sialic acid, constituting its terminal trisaccharides biantennary chains. N-Acetylneuraminic Acid 79-90 transferrin Homo sapiens 13-24 1590525-3 1992 Removal of sialic acid with neuraminidase revealed the same transferrin phenotypes as in their parents. N-Acetylneuraminic Acid 11-22 transferrin Homo sapiens 60-71 1946584-0 1991 Alcohol intoxication and sialic acid in erythrocyte membrane and in serum transferrin. N-Acetylneuraminic Acid 25-36 transferrin Homo sapiens 74-85 34562778-1 2021 Transferrin is a glycoprotein containing two bi- or tri-antennary carbohydrate chains ending with sialic acid. N-Acetylneuraminic Acid 98-109 transferrin Homo sapiens 0-11 34611562-5 2021 The molar absorption coefficients in the near-UV region for the native and desialylated apo-transferrin differ by several percent, suggesting a subtle dependence of the glycoprotein absorbance on the variable sialic acid content. N-Acetylneuraminic Acid 209-220 transferrin Homo sapiens 92-103 7840430-0 1994 [Multicenter study of sialic acid deficient transferrin determined by two chromatographic techniques]. N-Acetylneuraminic Acid 22-33 transferrin Homo sapiens 44-55 8403395-3 1993 Transferrin isoforms deficient in sialic acid, with pIs 5.7 and 5.9, can easily be separated and quantitated as a percentage of the total transferrin. N-Acetylneuraminic Acid 34-45 transferrin Homo sapiens 0-11 8403395-3 1993 Transferrin isoforms deficient in sialic acid, with pIs 5.7 and 5.9, can easily be separated and quantitated as a percentage of the total transferrin. N-Acetylneuraminic Acid 34-45 transferrin Homo sapiens 138-149 8330405-2 1993 We report a case of an allelic (polypeptide) variant of transferrin with mobility similar to that of the beta 2 (sialic acid-depleted) transferrin found in cerebrospinal fluid (CSF) and a few other body fluids. N-Acetylneuraminic Acid 113-124 transferrin Homo sapiens 56-67 8330405-2 1993 We report a case of an allelic (polypeptide) variant of transferrin with mobility similar to that of the beta 2 (sialic acid-depleted) transferrin found in cerebrospinal fluid (CSF) and a few other body fluids. N-Acetylneuraminic Acid 113-124 transferrin Homo sapiens 135-146 1555586-6 1992 The results demonstrate that human transferrin receptor from placenta predominantly carries diantennary and triantennary N-acetyllactosaminic glycans as well as hybrid-type species, the galactose residues of which being almost completely substituted with (alpha 2-3)-linked sialic acid residues. N-Acetylneuraminic Acid 274-285 transferrin Homo sapiens 35-46 3189316-9 1988 This study 1) confirmed that asialotransferrin-iron uptake by the hepatocyte is mediated by both transferrin and asialoglycoprotein receptors; 2) demonstrated that not only asialotransferrin but also transferrin of low sialic acid content will increase iron turnover and lead to excessive iron loading of the hepatocyte; 3) and showed that the intrahepatocyte metabolism of asialotransferrin-iron did not differ from that of iron delivered by normal transferrin. N-Acetylneuraminic Acid 219-230 transferrin Homo sapiens 35-46 2910347-0 1989 The N-acetylneuraminic acid content of five forms of human transferrin. N-Acetylneuraminic Acid 4-27 transferrin Homo sapiens 59-70 2910347-1 1989 Five isoforms of human serum transferrin were separated by isoelectric focusing and their N-acetylneuraminic acid content was determined. N-Acetylneuraminic Acid 90-113 transferrin Homo sapiens 29-40 2910347-7 1989 Comparison of the sialic acid content of the five transferrin forms and their carbohydrate structures showed that some of the forms expose terminal galactose without attracting the asialoglycoprotein receptors on hepatocytes. N-Acetylneuraminic Acid 18-29 transferrin Homo sapiens 50-61 3409533-2 1988 These transferrin forms differ in the carbohydrate parts, especially the amount of sialic acid. N-Acetylneuraminic Acid 83-94 transferrin Homo sapiens 6-17 3169252-1 1988 The sequential removal of N-acetylneuraminic acid from rabbit serum transferrin has been followed by urea-polyacrylamide gel electrophoresis. N-Acetylneuraminic Acid 26-49 transferrin Homo sapiens 68-79 3409533-4 1988 However, in alcoholics during abstinence the newly formed transferrin has a higher sialic acid content than most of the transferrin already present in the blood. N-Acetylneuraminic Acid 83-94 transferrin Homo sapiens 58-69 3409533-5 1988 This indicates that the elevated concentration of Tf5.7 with a low sialic acid content, found in alcoholics is not due to a defect at sialylation, but most probably caused by an impaired uptake of sialic acid-deficient transferrin by the hepatocytes due to membrane dysfunction. N-Acetylneuraminic Acid 197-208 transferrin Homo sapiens 219-230 3427589-4 1987 The value of the method for preparative purposes was demonstrated for sialic acid-containing carbohydrates obtained from human serotransferrin by hydrazinolysis. N-Acetylneuraminic Acid 70-81 transferrin Homo sapiens 127-142 3314559-10 1987 Successive loss of sialic acid is compatible with the presence of different transferrin forms, and our results indicate that the main differences between the serum transferrin forms from healthy and alcoholic individuals are in successive changes of the carbohydrate chains attached at positions 413 and 611. N-Acetylneuraminic Acid 19-30 transferrin Homo sapiens 76-87 3478423-1 1987 Transferrin is a serum glycoprotein which contains four sialic acid residues located at the end of two branched carbohydrate structures. N-Acetylneuraminic Acid 56-67 transferrin Homo sapiens 0-11 3478423-6 1987 These experiments support the hypothesis that the "ladder" banding pattern of transferrin observed in some case samples is due to the removal of sialic acid residues by bacterial or endogenous neuraminidase. N-Acetylneuraminic Acid 145-156 transferrin Homo sapiens 78-89 3478423-7 1987 These studies also demonstrate that partially desialidated transferrin variants cannot be clearly typed until the sialic acid is completely stripped from the transferrin molecule. N-Acetylneuraminic Acid 114-125 transferrin Homo sapiens 59-70 6543331-0 1984 Sialic acid-deficient serum and cerebrospinal fluid transferrin in a newly recognized genetic syndrome. N-Acetylneuraminic Acid 0-11 transferrin Homo sapiens 52-63 3557459-5 1987 Stepwise removal of N-acetyl-neuraminic acid (NANA) with neuraminidase revealed that the most cathodal variant TF DShinnanyo found in a Japanese family was characterized by having only two NANA residues. N-Acetylneuraminic Acid 20-44 transferrin Homo sapiens 111-113 3716020-0 1986 Determination of sialic acid residues in transferrin by oxidative-reductive immunoassay. N-Acetylneuraminic Acid 17-28 transferrin Homo sapiens 41-52 2437241-2 1987 Owing to its low content of sialic acid, beta 2-transferrin migrates more slowly than the main transferrin component (beta 1-transferrin) in electrophoresis. N-Acetylneuraminic Acid 28-39 transferrin Homo sapiens 48-59 3603925-1 1986 Transferrin was double-labeled, with its sialic acid residues being labeled with 3H and its protein part with either 125I or 59Fe. N-Acetylneuraminic Acid 41-52 transferrin Homo sapiens 0-11 4073011-0 1985 Transferrin sialic acid contents of patients with hereditary hemochromatosis. N-Acetylneuraminic Acid 12-23 transferrin Homo sapiens 0-11 6088317-1 1984 Preparative isoelectric focusing of human diferric transferrin preparations yielded seven bands with different isoelectric points, due to differences in sialic acid content. N-Acetylneuraminic Acid 153-164 transferrin Homo sapiens 51-62 6787617-2 1980 The abnormality consists of a selective increase of a cathodal transferrin component which is probably caused by a reduction of the sialic acid content. N-Acetylneuraminic Acid 132-143 transferrin Homo sapiens 63-74 7030111-0 1981 Evidence of a reduced sialic acid content in serum transferrin in male alcoholics. N-Acetylneuraminic Acid 22-33 transferrin Homo sapiens 51-62 7030111-2 1981 Certain indirect evidence has supported the assumption that the basis for the altered transferrin heterogeneity would be a reduced sialic acid content. N-Acetylneuraminic Acid 131-142 transferrin Homo sapiens 86-97 7030111-4 1981 The sialic acid content in transferrin was thereafter determined directly. N-Acetylneuraminic Acid 4-15 transferrin Homo sapiens 27-38 7030111-5 1981 Transferrin from alcoholic patients showed a 22% lower sialic acid concentration than control transferrin, which was highly significant. N-Acetylneuraminic Acid 55-66 transferrin Homo sapiens 0-11 7030111-6 1981 These data together with results from experiments with neuraminidase and galactose-binding lectin provide evidence that in alcoholism at least two sialic acid residues are missing in a significant fraction of serum transferrin. N-Acetylneuraminic Acid 147-158 transferrin Homo sapiens 215-226 7030111-7 1981 This observation may indicate that sialic acid residues are missing in a significant fraction of serum transferrin. N-Acetylneuraminic Acid 35-46 transferrin Homo sapiens 103-114 116481-5 1979 There is evidence of a reduced sialic acid content in the abnormal transferrin. N-Acetylneuraminic Acid 31-42 transferrin Homo sapiens 67-78 856748-3 1977 The data obtained indicate that the excess number of electrophoretic bands observed in transferrin from this source is due to the loss of carbohydrates which only affects sialic acid and none of the other sugar types. N-Acetylneuraminic Acid 171-182 transferrin Homo sapiens 87-98 928327-3 1977 To study the role played by sialic acids of transferrin molecule in the formation of complexes with insulin the author used transferrin untreated and treated with neuraminidase, an enzyme splitting the sialic acid molecules from grycoprotein specifically. N-Acetylneuraminic Acid 28-39 transferrin Homo sapiens 44-55 928327-5 1977 Transferrin devoid of sialic acid lost its capacity to form complexes with insulin. N-Acetylneuraminic Acid 22-33 transferrin Homo sapiens 0-11 928327-7 1977 The results of experiments with the use of neuraminidase demonstrated that sialic acid in donor transferrin molecule could be of great significance in the formation of an insulin-transferrin complex. N-Acetylneuraminic Acid 75-86 transferrin Homo sapiens 96-107 928327-7 1977 The results of experiments with the use of neuraminidase demonstrated that sialic acid in donor transferrin molecule could be of great significance in the formation of an insulin-transferrin complex. N-Acetylneuraminic Acid 75-86 transferrin Homo sapiens 179-190 856748-5 1977 The reason for the gradual loss of sialic acid from transferrin is unknown. N-Acetylneuraminic Acid 35-46 transferrin Homo sapiens 52-63 14112276-4 1963 The faint components migrated slightly more rapidly than the corresponding components in the stepwise pattern produced by the action of neuraminidase in removing sialic acid from transferrin. N-Acetylneuraminic Acid 162-173 transferrin Homo sapiens 179-190 5690539-6 1968 Transferrin has most of its carbohydrate in a single unit composed of 2 residues of mannose, 2 residues of galactose, 3 residues of N-acetylglucosamine and either 1 or 2 residues of sialic acid. N-Acetylneuraminic Acid 182-193 transferrin Homo sapiens 0-11 28236367-1 2018 BACKGROUND: Transferrin, a major glycoprotein has different isoforms depending on the number of sialic acid residues present on its oligosaccharide chain. N-Acetylneuraminic Acid 96-107 transferrin Homo sapiens 12-23 14483938-3 1962 These components appeared to represent the stepwise removal of the four sialic acid residues from the transferrin molecule, and at large enzyme concentrations, almost all of the transferrin was reduced to the position of the slowest moving component. N-Acetylneuraminic Acid 72-83 transferrin Homo sapiens 102-113 14483938-3 1962 These components appeared to represent the stepwise removal of the four sialic acid residues from the transferrin molecule, and at large enzyme concentrations, almost all of the transferrin was reduced to the position of the slowest moving component. N-Acetylneuraminic Acid 72-83 transferrin Homo sapiens 178-189 14483938-9 1962 The transferrin pattern of cord blood showed a prominent band in the position of transferrin C, accompanied by four faint slower moving bands which coincided with the four transferrin components produced by the action of neuraminidase on transferrin C. The transferrin pattern of cerebrospinal fluid in individuals homozygous for serum transferrin C showed two principal components, one of which appeared to contain no sialic acid. N-Acetylneuraminic Acid 419-430 transferrin Homo sapiens 4-15 13732863-0 1961 Alterations in sialic acid content of human transferrin. N-Acetylneuraminic Acid 15-26 transferrin Homo sapiens 44-55 13732863-2 1961 Sialic acid analysis after starch block electrophoresis suggested that the bands represented the stepwise removal of sialic acid from the transferrin molecule. N-Acetylneuraminic Acid 0-11 transferrin Homo sapiens 138-149 13732863-2 1961 Sialic acid analysis after starch block electrophoresis suggested that the bands represented the stepwise removal of sialic acid from the transferrin molecule. N-Acetylneuraminic Acid 117-128 transferrin Homo sapiens 138-149 30890358-1 2019 Asialo-human transferrin (asialo-hTf) is a glycoform of the human serum protein transferrin characterized by the lack of the sialic acid (SA) terminal unit. N-Acetylneuraminic Acid 125-136 transferrin Homo sapiens 13-24 30890358-1 2019 Asialo-human transferrin (asialo-hTf) is a glycoform of the human serum protein transferrin characterized by the lack of the sialic acid (SA) terminal unit. N-Acetylneuraminic Acid 125-136 transferrin Homo sapiens 80-91 30890358-1 2019 Asialo-human transferrin (asialo-hTf) is a glycoform of the human serum protein transferrin characterized by the lack of the sialic acid (SA) terminal unit. N-Acetylneuraminic Acid 138-140 transferrin Homo sapiens 13-24 30890358-1 2019 Asialo-human transferrin (asialo-hTf) is a glycoform of the human serum protein transferrin characterized by the lack of the sialic acid (SA) terminal unit. N-Acetylneuraminic Acid 138-140 transferrin Homo sapiens 80-91 27664951-3 2016 Aims of this study was to examine the influence of tobacco smoking on transferrin sialic acid residues and their connection with fetal biometric parameters in women with iron-deficiency. N-Acetylneuraminic Acid 82-93 transferrin Homo sapiens 70-81 27448041-3 2016 This study examines influence of tobacco smoking on transferrin sialic acid residues and its connection to foetal nourishment at women with iron deficiency. N-Acetylneuraminic Acid 64-75 transferrin Homo sapiens 52-63 23631694-11 2013 Oxidation of the sialic acid side chains of Tf generated aldehyde functionalized protein that was reacted with aminooxy terminated poly(HPMA), which resulted in protein-polymer bioconjugates carrying oxime linkages. N-Acetylneuraminic Acid 17-28 transferrin Homo sapiens 44-46 26335155-5 2016 We show mass spectrometric data combined with data from enzymatic digestions that suggest the presence of a tetrasaccharide consisting of two N-acetylglucosamines, one galactose, and one sialic acid, appearing on serum TF, is a biomarker of this particular CDG subtype. N-Acetylneuraminic Acid 187-198 transferrin Homo sapiens 219-221 23830432-5 2013 In addition, the approach was applied to characterize the sialylated status of alpha2-macroglobulin and transferrin, respectively, from the sera of healthy subjects and sex- and age-matched patients with thyroid cancer, and their spectra indicate that the change in the amount of the glycoforms containing different number of sialic acid (SA) residues from one glycosylation site may be used to differentiate between healthy subjects and cancer cases. N-Acetylneuraminic Acid 326-337 transferrin Homo sapiens 104-115 23830432-5 2013 In addition, the approach was applied to characterize the sialylated status of alpha2-macroglobulin and transferrin, respectively, from the sera of healthy subjects and sex- and age-matched patients with thyroid cancer, and their spectra indicate that the change in the amount of the glycoforms containing different number of sialic acid (SA) residues from one glycosylation site may be used to differentiate between healthy subjects and cancer cases. N-Acetylneuraminic Acid 339-341 transferrin Homo sapiens 104-115 22041858-8 2011 The investigation of the influence of sialic acid in the carbohydrate chain of human serum Tf, studied by incubating the protein with neuraminidase (sialidase) to obtain the monosialilated species, revealed that the binding affinity of Ti was similar for monosialo-Tf and for native-Tf and occurs in the N-lobe. N-Acetylneuraminic Acid 38-49 transferrin Homo sapiens 91-93 22041858-8 2011 The investigation of the influence of sialic acid in the carbohydrate chain of human serum Tf, studied by incubating the protein with neuraminidase (sialidase) to obtain the monosialilated species, revealed that the binding affinity of Ti was similar for monosialo-Tf and for native-Tf and occurs in the N-lobe. N-Acetylneuraminic Acid 38-49 transferrin Homo sapiens 265-267 22041858-8 2011 The investigation of the influence of sialic acid in the carbohydrate chain of human serum Tf, studied by incubating the protein with neuraminidase (sialidase) to obtain the monosialilated species, revealed that the binding affinity of Ti was similar for monosialo-Tf and for native-Tf and occurs in the N-lobe. N-Acetylneuraminic Acid 38-49 transferrin Homo sapiens 265-267 21663560-3 2011 Since samples from alcoholic patients are characterized by decreased sialic acid content in serum transferrin, the assessment of CDT is thereby widely used for laboratory evaluation of chronic alcohol abuse. N-Acetylneuraminic Acid 69-80 transferrin Homo sapiens 98-109