메뉴 건너뛰기




Volumn 21, Issue 2, 2006, Pages 79-90

Standardization of TSH immunoassays: production of new calibrators and harmonization of assays;Standardisation des immunodosages de la TSH : production de nouveaux calibrateurs et harmonisation des tests

Author keywords

Antigenic polymorphism; Glycosylation; Immunodiagnostic; TSH

Indexed keywords

EPITOPE; HYPOPHYSIS HORMONE; THYROTROPIN;

EID: 33747406591     PISSN: 09232532     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.immbio.2005.09.002     Document Type: Short Survey
Times cited : (4)

References (70)
  • 1
    • 0023195323 scopus 로고
    • Monoclonal antibody mapping of the antigenic surface of human thyrotropin and its subunits
    • Benkirane M.M., Bon D., Costagliola S., Paolucci F., Darbouret B., Prince P., et al. Monoclonal antibody mapping of the antigenic surface of human thyrotropin and its subunits. Endocrinology 121 3 (1987) 1171-1177
    • (1987) Endocrinology , vol.121 , Issue.3 , pp. 1171-1177
    • Benkirane, M.M.1    Bon, D.2    Costagliola, S.3    Paolucci, F.4    Darbouret, B.5    Prince, P.6
  • 2
    • 0034541779 scopus 로고    scopus 로고
    • A 3D model for the human hepatic asialoglycoprotein receptor (ASGP-R)
    • Bianucci A.M., and Chiellini F. A 3D model for the human hepatic asialoglycoprotein receptor (ASGP-R). J. Biomol. Struct. Dyn. 18 3 (2000) 435-451
    • (2000) J. Biomol. Struct. Dyn. , vol.18 , Issue.3 , pp. 435-451
    • Bianucci, A.M.1    Chiellini, F.2
  • 3
    • 0029103263 scopus 로고
    • Biological and immunochemical characterization of recombinant human thyrotrophin
    • Canonne C., Papandreou M.J., Medri G., Verrier B., and Ronin C. Biological and immunochemical characterization of recombinant human thyrotrophin. Glycobiology 5 5 (1995) 473-481
    • (1995) Glycobiology , vol.5 , Issue.5 , pp. 473-481
    • Canonne, C.1    Papandreou, M.J.2    Medri, G.3    Verrier, B.4    Ronin, C.5
  • 4
    • 0025370666 scopus 로고
    • Analytical and clinical performance of six sensitive thyrotrophin kits
    • Chan B.Y., and Swaminathan R. Analytical and clinical performance of six sensitive thyrotrophin kits. Pathology 22 1 (1990) 11-15
    • (1990) Pathology , vol.22 , Issue.1 , pp. 11-15
    • Chan, B.Y.1    Swaminathan, R.2
  • 5
    • 0027177562 scopus 로고
    • Recombinant human thyroid stimulating hormone: development of a biotechnology product for detection of metastatic lesions of thyroid carcinoma
    • Cole E.S., Lee K., Lauziere K., Kelton C., Chappel S., Weintraub B., et al. Recombinant human thyroid stimulating hormone: development of a biotechnology product for detection of metastatic lesions of thyroid carcinoma. Biotechnology (N. Y.) 11 9 (1993) 1014-1024
    • (1993) Biotechnology (N. Y.) , vol.11 , Issue.9 , pp. 1014-1024
    • Cole, E.S.1    Lee, K.2    Lauziere, K.3    Kelton, C.4    Chappel, S.5    Weintraub, B.6
  • 6
    • 0037318895 scopus 로고    scopus 로고
    • Laboratory medicine practice guidelines: laboratory support for the diagnosis and monitoring of thyroid disease
    • Demers L.M., and Spencer C.A. Laboratory medicine practice guidelines: laboratory support for the diagnosis and monitoring of thyroid disease. Clin. Endocrinol. (Oxf.) 58 2 (2003) 138-140
    • (2003) Clin. Endocrinol. (Oxf.) , vol.58 , Issue.2 , pp. 138-140
    • Demers, L.M.1    Spencer, C.A.2
  • 8
    • 23044467768 scopus 로고    scopus 로고
    • Both core and terminal glycosylation alter epitope expression in thyrotropin and introduce discordances in hormone measurements
    • Donadio S., Morelle W., Pascual A., Romi-Lebrun R., Michalski J.C., and Ronin C. Both core and terminal glycosylation alter epitope expression in thyrotropin and introduce discordances in hormone measurements. Clin. Chem. Lab. Med. 43 5 (2005) 519-530
    • (2005) Clin. Chem. Lab. Med. , vol.43 , Issue.5 , pp. 519-530
    • Donadio, S.1    Morelle, W.2    Pascual, A.3    Romi-Lebrun, R.4    Michalski, J.C.5    Ronin, C.6
  • 9
    • 0026342559 scopus 로고
    • Clearing up glycoprotein hormones
    • Drickamer K. Clearing up glycoprotein hormones. Cell 67 6 (1991) 1029-1032
    • (1991) Cell , vol.67 , Issue.6 , pp. 1029-1032
    • Drickamer, K.1
  • 10
    • 0026314891 scopus 로고
    • A hepatic reticuloendothelial cell receptor specific for SO4-4GalNAc beta 1,4GlcNAc beta 1,2Man alpha that mediates rapid clearance of lutropin
    • Fiete D., Srivastava V., Hindsgaul O., and Baenziger J.U. A hepatic reticuloendothelial cell receptor specific for SO4-4GalNAc beta 1,4GlcNAc beta 1,2Man alpha that mediates rapid clearance of lutropin. Cell 67 6 (1991) 1103-1110
    • (1991) Cell , vol.67 , Issue.6 , pp. 1103-1110
    • Fiete, D.1    Srivastava, V.2    Hindsgaul, O.3    Baenziger, J.U.4
  • 11
    • 8344271025 scopus 로고    scopus 로고
    • Advances in the production of human therapeutic proteins in yeasts and filamentous fungi
    • Gerngross T.U. Advances in the production of human therapeutic proteins in yeasts and filamentous fungi. Nat. Biotechnol. 22 11 (2004) 1409-1414
    • (2004) Nat. Biotechnol. , vol.22 , Issue.11 , pp. 1409-1414
    • Gerngross, T.U.1
  • 12
    • 0032848329 scopus 로고    scopus 로고
    • Genetic engineering of recombinant glycoproteins and the glycosylation pathway in mammalian host cells
    • Grabenhorst E., Schlenke P., Pohl S., Nimtz M., and Conradt H.S. Genetic engineering of recombinant glycoproteins and the glycosylation pathway in mammalian host cells. Glycoconj. J. 16 2 (1999) 81-97
    • (1999) Glycoconj. J. , vol.16 , Issue.2 , pp. 81-97
    • Grabenhorst, E.1    Schlenke, P.2    Pohl, S.3    Nimtz, M.4    Conradt, H.S.5
  • 13
    • 0031014551 scopus 로고    scopus 로고
    • Expression of biologically active human thyrotropin (hTSH) in a baculovirus system: effect of insect cell glycosylation on hTSH activity in vitro and in vivo
    • Grossmann M., Wong R., Teh N.G., Tropea J.E., East-Palmer J., Weintraub B.D., et al. Expression of biologically active human thyrotropin (hTSH) in a baculovirus system: effect of insect cell glycosylation on hTSH activity in vitro and in vivo. Endocrinology 138 1 (1997) 92-100
    • (1997) Endocrinology , vol.138 , Issue.1 , pp. 92-100
    • Grossmann, M.1    Wong, R.2    Teh, N.G.3    Tropea, J.E.4    East-Palmer, J.5    Weintraub, B.D.6
  • 14
    • 0023037088 scopus 로고
    • The ligand binding specificity and tissue localization of a rat alveolar macrophage lectin
    • Haltiwanger R.S., and Hill R.L. The ligand binding specificity and tissue localization of a rat alveolar macrophage lectin. J. Biol. Chem. 261 33 (1986) 15696-15702
    • (1986) J. Biol. Chem. , vol.261 , Issue.33 , pp. 15696-15702
    • Haltiwanger, R.S.1    Hill, R.L.2
  • 15
    • 0028355727 scopus 로고
    • Sialyltransferase messenger ribonucleic acid increases in thyrotrophs of hypothyroid mice: an in situ hybridization study
    • Helton T.E., and Magner J.A. Sialyltransferase messenger ribonucleic acid increases in thyrotrophs of hypothyroid mice: an in situ hybridization study. Endocrinology 134 6 (1994) 2347-2353
    • (1994) Endocrinology , vol.134 , Issue.6 , pp. 2347-2353
    • Helton, T.E.1    Magner, J.A.2
  • 16
    • 0028171316 scopus 로고
    • Beta-1,4-galactosyltransferase and alpha-mannosidase-II messenger ribonucleic acid levels increase with different kinetics in thyrotrophs of hypothyroid mice
    • Helton T.E., and Magner J.A. Beta-1,4-galactosyltransferase and alpha-mannosidase-II messenger ribonucleic acid levels increase with different kinetics in thyrotrophs of hypothyroid mice. Endocrinology 135 5 (1994) 1980-1985
    • (1994) Endocrinology , vol.135 , Issue.5 , pp. 1980-1985
    • Helton, T.E.1    Magner, J.A.2
  • 17
    • 0029152067 scopus 로고
    • beta-Galactoside alpha-2,3-sialyltransferase messenger RNA increases in thyrotrophs of hypothyroid mice
    • Helton T.E., and Magner J.A. beta-Galactoside alpha-2,3-sialyltransferase messenger RNA increases in thyrotrophs of hypothyroid mice. Thyroid 5 4 (1995) 315-317
    • (1995) Thyroid , vol.5 , Issue.4 , pp. 315-317
    • Helton, T.E.1    Magner, J.A.2
  • 18
    • 0026793042 scopus 로고
    • The asparagine-linked oligosaccharides at individual glycosylation sites in human thyrotrophin
    • Hiyama J., Weisshaar G., and Renwick A.G. The asparagine-linked oligosaccharides at individual glycosylation sites in human thyrotrophin. Glycobiology 2 5 (1992) 401-409
    • (1992) Glycobiology , vol.2 , Issue.5 , pp. 401-409
    • Hiyama, J.1    Weisshaar, G.2    Renwick, A.G.3
  • 19
    • 0016304913 scopus 로고
    • The isolation and properties of a rabbit liver binding protein specific for asialoglycoproteins
    • Hudgin R.L., Pricer Jr. W.E., Ashwell G., Stockert R.J., and Morell A.G. The isolation and properties of a rabbit liver binding protein specific for asialoglycoproteins. J. Biol. Chem. 249 17 (1974) 5536-5543
    • (1974) J. Biol. Chem. , vol.249 , Issue.17 , pp. 5536-5543
    • Hudgin, R.L.1    Pricer Jr., W.E.2    Ashwell, G.3    Stockert, R.J.4    Morell, A.G.5
  • 20
    • 0032727842 scopus 로고    scopus 로고
    • Effect of N-linked glycosylation on glycopeptide and glycoprotein structure
    • Imperiali B., and O'Connor S.E. Effect of N-linked glycosylation on glycopeptide and glycoprotein structure. Curr. Opin. Chem. Biol. 3 6 (1999) 643-649
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , Issue.6 , pp. 643-649
    • Imperiali, B.1    O'Connor, S.E.2
  • 22
    • 0033623288 scopus 로고    scopus 로고
    • alpha3-galactosylated glycoproteins can bind to the hepatic asialoglycoprotein receptor
    • Joziasse D.H., Lee R.T., Lee Y.C., Biessen E.A., Schiphorst W.E., Koeleman C.A., et al. alpha3-galactosylated glycoproteins can bind to the hepatic asialoglycoprotein receptor. Eur. J. Biochem. 267 21 (2000) 6501-6508
    • (2000) Eur. J. Biochem. , vol.267 , Issue.21 , pp. 6501-6508
    • Joziasse, D.H.1    Lee, R.T.2    Lee, Y.C.3    Biessen, E.A.4    Schiphorst, W.E.5    Koeleman, C.A.6
  • 23
    • 0025871151 scopus 로고
    • Immunological and biological characteristics of recombinant human thyrotropin
    • Kashiwai T., Ichihara K., Endo Y., Tamaki H., Amino N., and Miyai K. Immunological and biological characteristics of recombinant human thyrotropin. J. Immunol. Methods 143 1 (1991) 25-30
    • (1991) J. Immunol. Methods , vol.143 , Issue.1 , pp. 25-30
    • Kashiwai, T.1    Ichihara, K.2    Endo, Y.3    Tamaki, H.4    Amino, N.5    Miyai, K.6
  • 24
    • 0027729353 scopus 로고
    • Persistent problems with the specificity of immunometric TSH assays
    • Laurberg P. Persistent problems with the specificity of immunometric TSH assays. Thyroid 3 4 (1993) 279-283
    • (1993) Thyroid , vol.3 , Issue.4 , pp. 279-283
    • Laurberg, P.1
  • 25
    • 0022872679 scopus 로고
    • The binding of fucose-containing glycoproteins by hepatic lectins. The binding specificity of the rat liver fucose lectin
    • Lehrman M.A., Haltiwanger R.S., and Hill R.L. The binding of fucose-containing glycoproteins by hepatic lectins. The binding specificity of the rat liver fucose lectin. J. Biol. Chem. 261 16 (1986) 7426-7432
    • (1986) J. Biol. Chem. , vol.261 , Issue.16 , pp. 7426-7432
    • Lehrman, M.A.1    Haltiwanger, R.S.2    Hill, R.L.3
  • 26
    • 0036153437 scopus 로고    scopus 로고
    • Standardization: comparability and traceability of laboratory results
    • Lequin R.M. Standardization: comparability and traceability of laboratory results. Clin. Chem. 48 2 (2002) 391-393
    • (2002) Clin. Chem. , vol.48 , Issue.2 , pp. 391-393
    • Lequin, R.M.1
  • 27
    • 0036210522 scopus 로고    scopus 로고
    • The role of glycosylation in protein antigenic properties
    • Lisowska E. The role of glycosylation in protein antigenic properties. Cell. Mol. Life Sci. 59 3 (2002) 445-455
    • (2002) Cell. Mol. Life Sci. , vol.59 , Issue.3 , pp. 445-455
    • Lisowska, E.1
  • 28
    • 0027174451 scopus 로고
    • Endocytosis of ricin by rat liver cells in vivo and in vitro is mainly mediated by mannose receptors on sinusoidal endothelial cells
    • Magnusson S., and Berg T. Endocytosis of ricin by rat liver cells in vivo and in vitro is mainly mediated by mannose receptors on sinusoidal endothelial cells. Biochem. J. 291 3 (1993) 749-755
    • (1993) Biochem. J. , vol.291 , Issue.3 , pp. 749-755
    • Magnusson, S.1    Berg, T.2
  • 29
    • 0034697981 scopus 로고    scopus 로고
    • Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor
    • Meier M., Bider M.D., Malashkevich V.N., Spiess M., and Burkhard P. Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor. J. Mol. Biol. 300 4 (2000) 857-865
    • (2000) J. Mol. Biol. , vol.300 , Issue.4 , pp. 857-865
    • Meier, M.1    Bider, M.D.2    Malashkevich, V.N.3    Spiess, M.4    Burkhard, P.5
  • 30
    • 0024460892 scopus 로고
    • Concanavalin-A, lentil, and ricin lectin affinity binding characteristics of human thyrotropin: differences in the sialylation of thyrotropin in sera of euthyroid, primary, and central hypothyroid patients
    • Miura Y., Perkel V.S., Papenberg K.A., Johnson M.J., and Magner J.A. Concanavalin-A, lentil, and ricin lectin affinity binding characteristics of human thyrotropin: differences in the sialylation of thyrotropin in sera of euthyroid, primary, and central hypothyroid patients. J. Clin. Endocrinol. Metab. 69 5 (1989) 985-995
    • (1989) J. Clin. Endocrinol. Metab. , vol.69 , Issue.5 , pp. 985-995
    • Miura, Y.1    Perkel, V.S.2    Papenberg, K.A.3    Johnson, M.J.4    Magner, J.A.5
  • 31
    • 0019876887 scopus 로고
    • Isolation and characterization of a mannan-binding protein from rat liver
    • Mizuno Y., Kozutsumi Y., Kawasaki T., and Yamashina I. Isolation and characterization of a mannan-binding protein from rat liver. J. Biol. Chem. 256 9 (1981) 4247-4252
    • (1981) J. Biol. Chem. , vol.256 , Issue.9 , pp. 4247-4252
    • Mizuno, Y.1    Kozutsumi, Y.2    Kawasaki, T.3    Yamashina, I.4
  • 32
    • 0015217323 scopus 로고
    • The role of sialic acid in determining the survival of glycoproteins in the circulation
    • Morell A.G., Gregoriadis G., Scheinberg I.H., Hickman J., and Ashwell G. The role of sialic acid in determining the survival of glycoproteins in the circulation. J. Biol. Chem. 246 5 (1971) 1461-1467
    • (1971) J. Biol. Chem. , vol.246 , Issue.5 , pp. 1461-1467
    • Morell, A.G.1    Gregoriadis, G.2    Scheinberg, I.H.3    Hickman, J.4    Ashwell, G.5
  • 33
    • 0033636288 scopus 로고    scopus 로고
    • Implementation of reference systems in laboratory medicine
    • Müller M.M. Implementation of reference systems in laboratory medicine. Clin. Chem. 46 12 (2000) 1907-1909
    • (2000) Clin. Chem. , vol.46 , Issue.12 , pp. 1907-1909
    • Müller, M.M.1
  • 35
    • 0027483354 scopus 로고
    • Concanavalin A affinity chromatography of human serum gonadotropins: evidence for changes of carbohydrate structure in different clinical conditions
    • Papandreou M.J., Asteria C., Pettersson K., Ronin C., and Beck-Peccoz P. Concanavalin A affinity chromatography of human serum gonadotropins: evidence for changes of carbohydrate structure in different clinical conditions. J. Clin. Endocrinol. Metab. 76 4 (1993) 1008-1013
    • (1993) J. Clin. Endocrinol. Metab. , vol.76 , Issue.4 , pp. 1008-1013
    • Papandreou, M.J.1    Asteria, C.2    Pettersson, K.3    Ronin, C.4    Beck-Peccoz, P.5
  • 36
    • 0027261228 scopus 로고
    • Variable carbohydrate structures of circulating thyrotropin as studied by lectin affinity chromatography in different clinical conditions
    • Papandreou M.J., Persani L., Asteria C., Ronin C., and Beck-Peccoz P. Variable carbohydrate structures of circulating thyrotropin as studied by lectin affinity chromatography in different clinical conditions. J. Clin. Endocrinol. Metab. 77 2 (1993) 393-398
    • (1993) J. Clin. Endocrinol. Metab. , vol.77 , Issue.2 , pp. 393-398
    • Papandreou, M.J.1    Persani, L.2    Asteria, C.3    Ronin, C.4    Beck-Peccoz, P.5
  • 37
    • 0031786080 scopus 로고    scopus 로고
    • Changes in the degree of sialylation of carbohydrate chains modify the biological properties of circulating thyrotropin isoforms in various physiological and pathological states
    • Persani L., Borgato S., Romoli R., Asteria C., Pizzocaro A., and Beck-Peccoz P. Changes in the degree of sialylation of carbohydrate chains modify the biological properties of circulating thyrotropin isoforms in various physiological and pathological states. J. Clin. Endocrinol. Metab. 83 7 (1998) 2486-2492
    • (1998) J. Clin. Endocrinol. Metab. , vol.83 , Issue.7 , pp. 2486-2492
    • Persani, L.1    Borgato, S.2    Romoli, R.3    Asteria, C.4    Pizzocaro, A.5    Beck-Peccoz, P.6
  • 38
    • 0019729482 scopus 로고
    • Glycoprotein hormones: structure and function
    • Pierce J.G., and Parsons T.F. Glycoprotein hormones: structure and function. Annu. Rev. Biochem. 50 (1981) 465-495
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 465-495
    • Pierce, J.G.1    Parsons, T.F.2
  • 40
    • 0034771429 scopus 로고    scopus 로고
    • Functional sensitivity and recovery of thyroid-stimulating hormone
    • Price A., Burgin C., Catch I., and Cruise M. Functional sensitivity and recovery of thyroid-stimulating hormone. Clin. Chem. 47 11 (2001) 2067
    • (2001) Clin. Chem. , vol.47 , Issue.11 , pp. 2067
    • Price, A.1    Burgin, C.2    Catch, I.3    Cruise, M.4
  • 41
    • 0015218337 scopus 로고
    • The binding of desialylated glycoproteins by plasma membranes of rat liver
    • Pricer Jr. W.E., and Ashwell G. The binding of desialylated glycoproteins by plasma membranes of rat liver. J. Biol. Chem. 246 15 (1971) 4825-4833
    • (1971) J. Biol. Chem. , vol.246 , Issue.15 , pp. 4825-4833
    • Pricer Jr., W.E.1    Ashwell, G.2
  • 43
    • 0017861074 scopus 로고
    • Hepatic receptor that specifically binds oligosaccharides containing fucosyl alpha1 leads to 3 N-acetylglucosamine linkages
    • Prieels J.P., Pizzo S.V., Glasgow L.R., Paulson J.C., and Hill R.L. Hepatic receptor that specifically binds oligosaccharides containing fucosyl alpha1 leads to 3 N-acetylglucosamine linkages. Proc. Natl. Acad. Sci. USA 75 5 (1978) 2215-2219
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , Issue.5 , pp. 2215-2219
    • Prieels, J.P.1    Pizzo, S.V.2    Glasgow, L.R.3    Paulson, J.C.4    Hill, R.L.5
  • 44
    • 0033907887 scopus 로고    scopus 로고
    • Involvement of sugars in protein-protein interactions
    • Qasba P.K. Involvement of sugars in protein-protein interactions. Carbohydrates Polymers. 41 (2000) 293-309
    • (2000) Carbohydrates Polymers. , vol.41 , pp. 293-309
    • Qasba, P.K.1
  • 45
    • 0032708438 scopus 로고    scopus 로고
    • > Comparison of pituitary and recombinant human thyroid-stimulating hormone (rhTSH) in a multicenter collaborative study: establishment of the first World Health Organization reference reagent for rhTSH
    • Rafferty B., and Gaines Das R. > Comparison of pituitary and recombinant human thyroid-stimulating hormone (rhTSH) in a multicenter collaborative study: establishment of the first World Health Organization reference reagent for rhTSH. Clin. Chem. 45 12 (1999) 2207-2215
    • (1999) Clin. Chem. , vol.45 , Issue.12 , pp. 2207-2215
    • Rafferty, B.1    Gaines Das, R.2
  • 47
    • 9244238199 scopus 로고    scopus 로고
    • Performance characteristics of six third-generation assays for thyroid-stimulating hormone
    • Rawlins M.L., and Roberts W.L. Performance characteristics of six third-generation assays for thyroid-stimulating hormone. Clin. Chem. 50 12 (2004) 2338-2344
    • (2004) Clin. Chem. , vol.50 , Issue.12 , pp. 2338-2344
    • Rawlins, M.L.1    Roberts, W.L.2
  • 48
    • 0030027712 scopus 로고    scopus 로고
    • The use of recombinant human thyrotropin produced by Chinese hamster ovary cells for the preparation of immunoassay reagents
    • Ribela M.T., Bianco A.C., and Bartolini P. The use of recombinant human thyrotropin produced by Chinese hamster ovary cells for the preparation of immunoassay reagents. J. Clin. Endocrinol. Metab. 81 1 (1996) 249-256
    • (1996) J. Clin. Endocrinol. Metab. , vol.81 , Issue.1 , pp. 249-256
    • Ribela, M.T.1    Bianco, A.C.2    Bartolini, P.3
  • 50
    • 0028931112 scopus 로고
    • Serum thyrotropin (TSH) heterogeneity in euthyroid subjects and patients with subclinical hypothyroidism: the core fucose content of TSH-releasing hormone-released TSH is altered, but not the net charge of TSH
    • Schaaf L., Trojan J., Helton T.E., Usadel K.H., and Magner J.A. Serum thyrotropin (TSH) heterogeneity in euthyroid subjects and patients with subclinical hypothyroidism: the core fucose content of TSH-releasing hormone-released TSH is altered, but not the net charge of TSH. J. Endocrinol. 144 3 (1995) 561-571
    • (1995) J. Endocrinol. , vol.144 , Issue.3 , pp. 561-571
    • Schaaf, L.1    Trojan, J.2    Helton, T.E.3    Usadel, K.H.4    Magner, J.A.5
  • 51
    • 0033916773 scopus 로고    scopus 로고
    • Thyrotropin-releasing hormone time-dependently influences thyrotropin microheterogeneity--an in vivo study in euthyroidism
    • Schaaf L., Theodoropoulou M., Gregori A., Leiprecht A., Trojan J., Klostermeier J., et al. Thyrotropin-releasing hormone time-dependently influences thyrotropin microheterogeneity--an in vivo study in euthyroidism. J. Endocrinol. 166 1 (2000) 137-143
    • (2000) J. Endocrinol. , vol.166 , Issue.1 , pp. 137-143
    • Schaaf, L.1    Theodoropoulou, M.2    Gregori, A.3    Leiprecht, A.4    Trojan, J.5    Klostermeier, J.6
  • 52
    • 0019214256 scopus 로고
    • The role of extra-hepatic tissues in the receptor-mediated plasma clearance of glycoproteins terminated by mannose or N-acetylglucosamine
    • Schlesinger P.H., Rodman J.S., Doebber T.W., Stahl P.D., Lee Y.C., Stowell C.P., et al. The role of extra-hepatic tissues in the receptor-mediated plasma clearance of glycoproteins terminated by mannose or N-acetylglucosamine. Biochem. J. 192 2 (1980) 597-606
    • (1980) Biochem. J. , vol.192 , Issue.2 , pp. 597-606
    • Schlesinger, P.H.1    Rodman, J.S.2    Doebber, T.W.3    Stahl, P.D.4    Lee, Y.C.5    Stowell, C.P.6
  • 53
    • 0039174268 scopus 로고    scopus 로고
    • Glycopeptide synthesis and the effects of glycosylation on protein structure and activity
    • Seitz O. Glycopeptide synthesis and the effects of glycosylation on protein structure and activity. ChemBioChem 1 4 (2000) 214-246
    • (2000) ChemBioChem , vol.1 , Issue.4 , pp. 214-246
    • Seitz, O.1
  • 56
    • 0025149128 scopus 로고
    • Circulating C-terminal propeptide of type I procollagen is cleared mainly via the mannose receptor in liver endothelial cells
    • Smedsrod B., Melkko J., Risteli L., and Risteli J. Circulating C-terminal propeptide of type I procollagen is cleared mainly via the mannose receptor in liver endothelial cells. Biochem. J. 271 2 (1990) 345-350
    • (1990) Biochem. J. , vol.271 , Issue.2 , pp. 345-350
    • Smedsrod, B.1    Melkko, J.2    Risteli, L.3    Risteli, J.4
  • 57
    • 0028938960 scopus 로고
    • Interlaboratory/intermethod differences in functional sensitivity of immunometric assays of thyrotropin (TSH) and impact on reliability of measurement of subnormal concentrations of TSH
    • Spencer C.A., Takeuchi M., Kazarosyan M., MacKenzie F., Beckett G.J., and Wilkinson E. Interlaboratory/intermethod differences in functional sensitivity of immunometric assays of thyrotropin (TSH) and impact on reliability of measurement of subnormal concentrations of TSH. Clin. Chem. 41 3 (1995) 367-374
    • (1995) Clin. Chem. , vol.41 , Issue.3 , pp. 367-374
    • Spencer, C.A.1    Takeuchi, M.2    Kazarosyan, M.3    MacKenzie, F.4    Beckett, G.J.5    Wilkinson, E.6
  • 58
    • 0035043203 scopus 로고    scopus 로고
    • Immunoassay standardization: is it possible, who is responsible, who is capable?
    • Stenman U.H. Immunoassay standardization: is it possible, who is responsible, who is capable?. Clin. Chem. 47 5 (2001) 815-820
    • (2001) Clin. Chem. , vol.47 , Issue.5 , pp. 815-820
    • Stenman, U.H.1
  • 59
    • 0027517557 scopus 로고
    • Purification and characterization of recombinant human thyrotropin (TSH) isoforms produced by Chinese hamster ovary cells: the role of sialylation and sulfation in TSH bioactivity
    • Szkudlinski M.W., Thotakura N.R., Bucci I., Joshi L.R., Tsai A., East-Palmer J., et al. Purification and characterization of recombinant human thyrotropin (TSH) isoforms produced by Chinese hamster ovary cells: the role of sialylation and sulfation in TSH bioactivity. Endocrinology 133 4 (1993) 1490-1503
    • (1993) Endocrinology , vol.133 , Issue.4 , pp. 1490-1503
    • Szkudlinski, M.W.1    Thotakura, N.R.2    Bucci, I.3    Joshi, L.R.4    Tsai, A.5    East-Palmer, J.6
  • 60
    • 0029112363 scopus 로고
    • Asparagine-linked oligosaccharide structures determine clearance and organ distribution of pituitary and recombinant thyrotropin
    • Szkudlinski M.W., Thotakura N.R., Tropea J.E., Grossmann M., and Weintraub B.D. Asparagine-linked oligosaccharide structures determine clearance and organ distribution of pituitary and recombinant thyrotropin. Endocrinology 136 8 (1995) 3325-3330
    • (1995) Endocrinology , vol.136 , Issue.8 , pp. 3325-3330
    • Szkudlinski, M.W.1    Thotakura, N.R.2    Tropea, J.E.3    Grossmann, M.4    Weintraub, B.D.5
  • 61
    • 0029079758 scopus 로고
    • Subunit-specific functions of N-linked oligosaccharides in human thyrotropin: role of terminal residues of alpha- and beta-subunit oligosaccharides in metabolic clearance and bioactivity
    • Szkudlinski M.W., Thotakura N.R., and Weintraub B.D. Subunit-specific functions of N-linked oligosaccharides in human thyrotropin: role of terminal residues of alpha- and beta-subunit oligosaccharides in metabolic clearance and bioactivity. Proc. Natl. Acad. Sci. USA 92 20 (1995) 9062-9066
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , Issue.20 , pp. 9062-9066
    • Szkudlinski, M.W.1    Thotakura, N.R.2    Weintraub, B.D.3
  • 62
    • 0025974324 scopus 로고
    • Biological activity and metabolic clearance of a recombinant human thyrotropin produced in Chinese hamster ovary cells
    • Thotakura N.R., Desai R.K., Bates L.G., Cole E.S., Pratt B.M., and Weintraub B.D. Biological activity and metabolic clearance of a recombinant human thyrotropin produced in Chinese hamster ovary cells. Endocrinology 128 1 (1991) 341-348
    • (1991) Endocrinology , vol.128 , Issue.1 , pp. 341-348
    • Thotakura, N.R.1    Desai, R.K.2    Bates, L.G.3    Cole, E.S.4    Pratt, B.M.5    Weintraub, B.D.6
  • 63
    • 0028078070 scopus 로고
    • Accuracy in clinical chemistry--does anybody care?
    • Tietz N.W. Accuracy in clinical chemistry--does anybody care?. Clin. Chem. 40 6 (1994) 859-861
    • (1994) Clin. Chem. , vol.40 , Issue.6 , pp. 859-861
    • Tietz, N.W.1
  • 64
    • 0019463053 scopus 로고
    • Isolation and characterization of a mannose/N-acetylglucosamine/fucose-binding protein from rat liver
    • Townsend R., and Stahl P. Isolation and characterization of a mannose/N-acetylglucosamine/fucose-binding protein from rat liver. Biochem. J. 194 1 (1981) 209-214
    • (1981) Biochem. J. , vol.194 , Issue.1 , pp. 209-214
    • Townsend, R.1    Stahl, P.2
  • 65
    • 0031652746 scopus 로고    scopus 로고
    • Modulation of human thyrotropin oligosaccharide structures--enhanced proportion of sialylated and terminally galactosylated serum thyrotropin isoforms in subclinical and overt primary hypothyroidism
    • Trojan J., Theodoropoulou M., Usadel K.H., Stalla G.K., and Schaaf L. Modulation of human thyrotropin oligosaccharide structures--enhanced proportion of sialylated and terminally galactosylated serum thyrotropin isoforms in subclinical and overt primary hypothyroidism. J. Endocrinol. 158 3 (1998) 359-365
    • (1998) J. Endocrinol. , vol.158 , Issue.3 , pp. 359-365
    • Trojan, J.1    Theodoropoulou, M.2    Usadel, K.H.3    Stalla, G.K.4    Schaaf, L.5
  • 66
    • 0015088424 scopus 로고
    • Effects of progressive desialylation on the rate of disappearance of immunoreactive HCG from plasma in rats
    • Van Hall E.V., Vaitukaitis J.L., Ross G.T., Hickman J.W., and Ashwell G. Effects of progressive desialylation on the rate of disappearance of immunoreactive HCG from plasma in rats. Endocrinology 89 1 (1971) 11-15
    • (1971) Endocrinology , vol.89 , Issue.1 , pp. 11-15
    • Van Hall, E.V.1    Vaitukaitis, J.L.2    Ross, G.T.3    Hickman, J.W.4    Ashwell, G.5
  • 67
    • 0034956803 scopus 로고    scopus 로고
    • Intramolecular carbohydrate-protein interaction
    • Vliegenthart J.F. Intramolecular carbohydrate-protein interaction. Adv. Exp. Med. Biol. 491 (2001) 133-140
    • (2001) Adv. Exp. Med. Biol. , vol.491 , pp. 133-140
    • Vliegenthart, J.F.1
  • 68
    • 0022186560 scopus 로고
    • An evaluation of six solid-phase thyrotropin (TSH) kits
    • Wood W.G., Waller D., and Hantke U. An evaluation of six solid-phase thyrotropin (TSH) kits. J. Clin. Chem. Clin. Biochem. 23 8 (1985) 461-471
    • (1985) J. Clin. Chem. Clin. Biochem. , vol.23 , Issue.8 , pp. 461-471
    • Wood, W.G.1    Waller, D.2    Hantke, U.3
  • 69
    • 0030026540 scopus 로고    scopus 로고
    • Evaluation of the Abbott IMx ultrasensitive II hTSH immunometric assay in three European centres: a comparison with established commercial immunometric assays for thyrotropin
    • Wood W.G., Bruns U., Eber O., Langsteger W., Bounaud J.Y., and Bounaud M.P. Evaluation of the Abbott IMx ultrasensitive II hTSH immunometric assay in three European centres: a comparison with established commercial immunometric assays for thyrotropin. Eur. J. Clin. Chem. Clin. Biochem. 34 2 (1996) 151-158
    • (1996) Eur. J. Clin. Chem. Clin. Biochem. , vol.34 , Issue.2 , pp. 151-158
    • Wood, W.G.1    Bruns, U.2    Eber, O.3    Langsteger, W.4    Bounaud, J.Y.5    Bounaud, M.P.6
  • 70
    • 0029756199 scopus 로고    scopus 로고
    • Glycosylation is the structural basis for changes in polymorphism and immunoreactivity of pituitary glycoprotein hormones
    • Zerfaoui M., and Ronin C. Glycosylation is the structural basis for changes in polymorphism and immunoreactivity of pituitary glycoprotein hormones. Eur. J. Clin. Chem. Clin. Biochem. 34 9 (1996) 749-753
    • (1996) Eur. J. Clin. Chem. Clin. Biochem. , vol.34 , Issue.9 , pp. 749-753
    • Zerfaoui, M.1    Ronin, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.