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Volumn 137, Issue 6, 1996, Pages 2543-2557

Oligosaccharide Mapping Reveals Hormone-Specific Glycosylation Patterns on Equine Gonadotropin α-Subunit Asn56

Author keywords

[No Author keywords available]

Indexed keywords

GONADOTROPIN;

EID: 0030004304     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.137.6.8641208     Document Type: Article
Times cited : (22)

References (63)
  • 1
    • 0019729482 scopus 로고
    • Glycoprotein hormones: Structure and function
    • Pierce JG, Parsons TF 1981 Glycoprotein hormones: structure and function. Annu Rev Biochem 50:465-490
    • (1981) Annu Rev Biochem , vol.50 , pp. 465-490
    • Pierce, J.G.1    Parsons, T.F.2
  • 2
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein
    • Wu H, Lustbader JW, Liu Y, Canfield RE, Hendrickson WA 1994 Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein. Structure 2:545-558
    • (1994) Structure , vol.2 , pp. 545-558
    • Wu, H.1    Lustbader, J.W.2    Liu, Y.3    Canfield, R.E.4    Hendrickson, W.A.5
  • 4
    • 0000676471 scopus 로고
    • Gonadotropins: Chemistry and biosynthesis
    • Knobil E, Neill JD (eds) Raven Press, New York
    • Bousfield GR, Perry WM, Ward DN 1994 Gonadotropins: chemistry and biosynthesis. In: Knobil E, Neill JD (eds) The Physiology of Reproduction. Raven Press, New York, p 1749-1792
    • (1994) The Physiology of Reproduction , pp. 1749-1792
    • Bousfield, G.R.1    Perry, W.M.2    Ward, D.N.3
  • 5
    • 0028890259 scopus 로고
    • Glycoprotein hormones: Glycobiology of gonadotrophins, thyrotrophin and free α subunit
    • Thotakura NR, Blithe DL 1995 Glycoprotein hormones: glycobiology of gonadotrophins, thyrotrophin and free α subunit. Glycobiology 5:3-10
    • (1995) Glycobiology , vol.5 , pp. 3-10
    • Thotakura, N.R.1    Blithe, D.L.2
  • 6
    • 0026585325 scopus 로고
    • Circulatory half-life but not interaction with the lutropin/ chorionic gonadotropin receptor is modulated by sulfation of bovine lutropin oligosaccharides
    • Baenziger JU, Kumar S, Brodbeck RM, Smith PL, Beranek MC 1992 Circulatory half-life but not interaction with the lutropin/ chorionic gonadotropin receptor is modulated by sulfation of bovine lutropin oligosaccharides. Proc Natl Acad Sci USA 89:334-338
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 334-338
    • Baenziger, J.U.1    Kumar, S.2    Brodbeck, R.M.3    Smith, P.L.4    Beranek, M.C.5
  • 7
    • 0015217323 scopus 로고
    • The role of sialic acid in determining the survival of glycoproteins in the circulation
    • Morell AG, Gregoriadis G, Scheinberg IH, Hickman J, Ashwell G 1971 The role of sialic acid in determining the survival of glycoproteins in the circulation. J Biol Chem 246:1461-1467
    • (1971) J Biol Chem , vol.246 , pp. 1461-1467
    • Morell, A.G.1    Gregoriadis, G.2    Scheinberg, I.H.3    Hickman, J.4    Ashwell, G.5
  • 8
    • 0019786696 scopus 로고
    • Effect of deglycosylation on the subunit interactions and receptor binding activity of human chorionic gonadotropin
    • Kalyan NK, Bahl OP 1981 Effect of deglycosylation on the subunit interactions and receptor binding activity of human chorionic gonadotropin. Biochem Biophys Res Commun 102:1246-1253
    • (1981) Biochem Biophys Res Commun , vol.102 , pp. 1246-1253
    • Kalyan, N.K.1    Bahl, O.P.2
  • 9
    • 0021749810 scopus 로고
    • Effect of desialylation of human chorionic gonadotropin on its metabolic clearance rate in humans
    • Rosa C, Amr S, Birken S, Wehmann R, Nisula B 1984 Effect of desialylation of human chorionic gonadotropin on its metabolic clearance rate in humans. J Clin Endocrinol Metab 59:1215-1219
    • (1984) J Clin Endocrinol Metab , vol.59 , pp. 1215-1219
    • Rosa, C.1    Amr, S.2    Birken, S.3    Wehmann, R.4    Nisula, B.5
  • 11
    • 0020426099 scopus 로고
    • Enzymatic deglycosylation of the subunits of chorionic gonadotropin: Effects on formation of tertiary structure and biological activity
    • Governman JM, Parsons TF, Pierce JG 1982 Enzymatic deglycosylation of the subunits of chorionic gonadotropin: effects on formation of tertiary structure and biological activity. J Biol Chem 257:15059-15064
    • (1982) J Biol Chem , vol.257 , pp. 15059-15064
    • Governman, J.M.1    Parsons, T.F.2    Pierce, J.G.3
  • 12
    • 0020621901 scopus 로고
    • Chemically deglycosylated human chorionic gonadotropin subunits: Characterization and biological properties
    • Keutmann HT, McIlroy PJ, Bergert ER, Ryan RJ 1983 Chemically deglycosylated human chorionic gonadotropin subunits: characterization and biological properties. Biochemistry 22:3067-3072
    • (1983) Biochemistry , vol.22 , pp. 3067-3072
    • Keutmann, H.T.1    McIlroy, P.J.2    Bergert, E.R.3    Ryan, R.J.4
  • 13
    • 0021235638 scopus 로고
    • Deglycosylated ovine lutropin: Preparation and characterization by in vitro binding and steroidogenesis
    • Liu WK, Young JD, Ward DN 1984 Deglycosylated ovine lutropin: preparation and characterization by in vitro binding and steroidogenesis. Mol Cell Endocrinol 37:29-39
    • (1984) Mol Cell Endocrinol , vol.37 , pp. 29-39
    • Liu, W.K.1    Young, J.D.2    Ward, D.N.3
  • 14
    • 0024511030 scopus 로고
    • Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction
    • Matzuk MM, Keene JL, Boime I 1989 Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction. J Biol Chem 264:2409-2414
    • (1989) J Biol Chem , vol.264 , pp. 2409-2414
    • Matzuk, M.M.1    Keene, J.L.2    Boime, I.3
  • 15
    • 0028289785 scopus 로고
    • Specific roles for the asparagine-linked carbohydrate residues of recombinant human follicle stimulating hormone in receptor binding and signal transduction
    • Bishop LA, Robertson DM, Cahir N, Schofield PR 1994 Specific roles for the asparagine-linked carbohydrate residues of recombinant human follicle stimulating hormone in receptor binding and signal transduction. J Mol Endocrinol 8:722-731
    • (1994) J Mol Endocrinol , vol.8 , pp. 722-731
    • Bishop, L.A.1    Robertson, D.M.2    Cahir, N.3    Schofield, P.R.4
  • 16
    • 0028358162 scopus 로고
    • Site-directed mutagenesis defines the individual roles of the glycosylation sites on follicle-stimulating hormone
    • Flack MR, Froehlich J, Bennet AP, Anasti J, Nisula BC 1994 Site-directed mutagenesis defines the individual roles of the glycosylation sites on follicle-stimulating hormone. J Biol Chem 269:14015-14020
    • (1994) J Biol Chem , vol.269 , pp. 14015-14020
    • Flack, M.R.1    Froehlich, J.2    Bennet, A.P.3    Anasti, J.4    Nisula, B.C.5
  • 17
    • 0020699583 scopus 로고
    • Hormonal antagonistic properties of chemically deglycosylated human choriogonadotropin
    • Sairam MR 1983 Hormonal antagonistic properties of chemically deglycosylated human choriogonadotropin. J Biol Chem 258:445-449
    • (1983) J Biol Chem , vol.258 , pp. 445-449
    • Sairam, M.R.1
  • 18
    • 0020683104 scopus 로고
    • Role of carbohydrate in human chorionic gonadotropin: Effect of deglycosylation on the subunit interaction and on its in vitro and in vivo biological properties
    • Kalyan NK, Bahl OP 1983 Role of carbohydrate in human chorionic gonadotropin: effect of deglycosylation on the subunit interaction and on its in vitro and in vivo biological properties. J Biol Chem 258:67-74
    • (1983) J Biol Chem , vol.258 , pp. 67-74
    • Kalyan, N.K.1    Bahl, O.P.2
  • 19
    • 0022256842 scopus 로고
    • Inhibition of adenylyl cyclase activity in rat corpora luteal tissue by glycopeptides of human chorionic gonadotropin and the α-subunit of human chorionic gonadotropin
    • Calvo FO, Ryan RJ 1985 Inhibition of adenylyl cyclase activity in rat corpora luteal tissue by glycopeptides of human chorionic gonadotropin and the α-subunit of human chorionic gonadotropin. Biochemistry 24:1953-1959
    • (1985) Biochemistry , vol.24 , pp. 1953-1959
    • Calvo, F.O.1    Ryan, R.J.2
  • 21
    • 0021189137 scopus 로고
    • Demonstration of peptide N-glycosidase F activity in endo-β-N-acetylglucosaminidase F preparations
    • Plummer TH, Elder JH, Alexander S, Phelan AW, Tarentino AL 1984 Demonstration of peptide N-glycosidase F activity in endo-β-N-acetylglucosaminidase F preparations. J Biol Chem 259:10700-10704
    • (1984) J Biol Chem , vol.259 , pp. 10700-10704
    • Plummer, T.H.1    Elder, J.H.2    Alexander, S.3    Phelan, A.W.4    Tarentino, A.L.5
  • 22
    • 0022003140 scopus 로고
    • Deglycosylation of asparagine-linked glycans by peptide-N-glycosidase F
    • Tarentino AL, Gómez CM, Plummer TH, Jr 1985 Deglycosylation of asparagine-linked glycans by peptide-N-glycosidase F. Biochemistry 24:4665-4671
    • (1985) Biochemistry , vol.24 , pp. 4665-4671
    • Tarentino, A.L.1    Gómez, C.M.2    Plummer Jr., T.H.3
  • 24
    • 0023217901 scopus 로고
    • Carbohydrate chains of human thyrotropin are differentially susceptible to endoglycosidase removal on combined and free polypeptide subunits
    • Ronin C, Papandreou M-J, Canonne C, Weintraub BD 1987 Carbohydrate chains of human thyrotropin are differentially susceptible to endoglycosidase removal on combined and free polypeptide subunits. Biochemistry 26:5848-5853
    • (1987) Biochemistry , vol.26 , pp. 5848-5853
    • Ronin, C.1    Papandreou, M.-J.2    Canonne, C.3    Weintraub, B.D.4
  • 25
    • 0023808074 scopus 로고
    • Differential susceptibility to N-glycanase at the individual glycosylation sites of mouse thyrotropin and free α-subunits
    • Miura Y, Perkel VS, Magner JA 1988 Differential susceptibility to N-glycanase at the individual glycosylation sites of mouse thyrotropin and free α-subunits. Endocrinology 123:2207-2213
    • (1988) Endocrinology , vol.123 , pp. 2207-2213
    • Miura, Y.1    Perkel, V.S.2    Magner, J.A.3
  • 26
    • 0025992391 scopus 로고
    • Site-specific N-gly-cosylation of human chorionic gonadotropin - Structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy
    • Weisshaar G, Hiyama J, Renwick AGC 1991 Site-specific N-gly-cosylation of human chorionic gonadotropin - structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy. Glycobiology 1:393-404
    • (1991) Glycobiology , vol.1 , pp. 393-404
    • Weisshaar, G.1    Hiyama, J.2    Renwick, A.G.C.3
  • 27
    • 0025976986 scopus 로고
    • NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin
    • Weisshaar G, Hiyama J, Renwick AGC, Nimtz M 1991 NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin. Eur J Biochem 195:257-268
    • (1991) Eur J Biochem , vol.195 , pp. 257-268
    • Weisshaar, G.1    Hiyama, J.2    Renwick, A.G.C.3    Nimtz, M.4
  • 28
    • 0024991081 scopus 로고
    • Site-specific N-gly-cosylation of ovine lutropin: Structural analysis by one- and two-dimensional 1H-NMR spectroscopy
    • Weisshaar G, Hiyama J, Renwick AGC 1990 Site-specific N-gly-cosylation of ovine lutropin: structural analysis by one- and two-dimensional 1H-NMR spectroscopy. Eur J Biochem 192:741-751
    • (1990) Eur J Biochem , vol.192 , pp. 741-751
    • Weisshaar, G.1    Hiyama, J.2    Renwick, A.G.C.3
  • 29
    • 0342976375 scopus 로고
    • Separation of positional isomers of oligosaccharides and glycopeptides by high-performance anion-exchange chromatography with pulsed amperometric detection
    • Hardy MR, Townsend RR 1988 Separation of positional isomers of oligosaccharides and glycopeptides by high-performance anion-exchange chromatography with pulsed amperometric detection. Proc Natl Acad Sci USA 85:3289-3293
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3289-3293
    • Hardy, M.R.1    Townsend, R.R.2
  • 30
    • 84995902802 scopus 로고
    • On the biological properties of highly purified gonadotropin from pregnant mare serum
    • Cole HH, Pencharz RI, Goss H 1946 On the biological properties of highly purified gonadotropin from pregnant mare serum. Endocrinology 27:548-553
    • (1946) Endocrinology , vol.27 , pp. 548-553
    • Cole, H.H.1    Pencharz, R.I.2    Goss, H.3
  • 31
    • 0026099739 scopus 로고
    • Equine chorionic gonadotropin
    • Murphy BD, Martinuk SD 1991 Equine chorionic gonadotropin. Endocr Rev 12:27-44
    • (1991) Endocr Rev , vol.12 , pp. 27-44
    • Murphy, B.D.1    Martinuk, S.D.2
  • 32
    • 0021869079 scopus 로고
    • Priming procedure and hormone preparations influence rat granulosa cell response
    • Liu W-K, Bousfield GR, Moore WT, Jr, Ward DN 1985 Priming procedure and hormone preparations influence rat granulosa cell response. Endocrinology 116:1454-1459
    • (1985) Endocrinology , vol.116 , pp. 1454-1459
    • Liu, W.-K.1    Bousfield, G.R.2    Moore Jr., W.T.3    Ward, D.N.4
  • 33
    • 0022969822 scopus 로고
    • Properties of equine luteinizing hormone alpha subunit alone and in combination with various subunits
    • Roser JF, Carrick FN, Papkoff H 1986 Properties of equine luteinizing hormone alpha subunit alone and in combination with various subunits. Biol Reprod 35:493-500
    • (1986) Biol Reprod , vol.35 , pp. 493-500
    • Roser, J.F.1    Carrick, F.N.2    Papkoff, H.3
  • 34
    • 0021353964 scopus 로고
    • Purification of lutropin and follitropin in high yield from horse pituitary glands
    • Bousfield GR, Ward DN 1984 Purification of lutropin and follitropin in high yield from horse pituitary glands. J Biol Chem 259: 1911-1921
    • (1984) J Biol Chem , vol.259 , pp. 1911-1921
    • Bousfield, G.R.1    Ward, D.N.2
  • 35
    • 0019314390 scopus 로고
    • Pregnant mare serum gonadotropin: Rapid isolation procedures for the purification of intact hormone and isolation of subunits
    • Moore WT, Jr, Ward DN 1980 Pregnant mare serum gonadotropin: rapid isolation procedures for the purification of intact hormone and isolation of subunits. J Biol Chem 255:6923-6929
    • (1980) J Biol Chem , vol.255 , pp. 6923-6929
    • Moore Jr., W.T.1    Ward, D.N.2
  • 36
    • 0026475001 scopus 로고
    • Reduction and reoxidation of equine gonadotropin α subunits
    • Bousfield GR, Ward DN 1992 Reduction and reoxidation of equine gonadotropin α subunits. Endocrinology 131:2986-2998
    • (1992) Endocrinology , vol.131 , pp. 2986-2998
    • Bousfield, G.R.1    Ward, D.N.2
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 0026051641 scopus 로고
    • Glycosylation sites identified by detection of glycosylated amino acids released from Edman degradation: The detection of Xaa-Pro-Xaa-Xaa as a motif for Thr O-glycosylation
    • Gooley AA, Classon BJ, Marschalek R, Williams KL 1991 Glycosylation sites identified by detection of glycosylated amino acids released from Edman degradation: the detection of Xaa-Pro-Xaa-Xaa as a motif for Thr O-glycosylation. Biochem Biophys Res Commun 178:1194-1201
    • (1991) Biochem Biophys Res Commun , vol.178 , pp. 1194-1201
    • Gooley, A.A.1    Classon, B.J.2    Marschalek, R.3    Williams, K.L.4
  • 39
    • 0023877998 scopus 로고
    • Monosaccharide analysis of glycoconjugates by anion exchange chromatograpy with pulsed amperometric detection
    • Hardy MR, Townsend RR, Lee YC 1988 Monosaccharide analysis of glycoconjugates by anion exchange chromatograpy with pulsed amperometric detection. Anal Biochem 170:54-62
    • (1988) Anal Biochem , vol.170 , pp. 54-62
    • Hardy, M.R.1    Townsend, R.R.2    Lee, Y.C.3
  • 40
    • 0025280694 scopus 로고
    • Carbohydrate composition of the α-subunit of human choriogonadotropin (hCGα) and the tree α molecules produced in pregnancy: Most free α and some combined hCGα molecules are fucosylated
    • Blithe DL 1990 Carbohydrate composition of the α-subunit of human choriogonadotropin (hCGα) and the tree α molecules produced in pregnancy: most free α and some combined hCGα molecules are fucosylated. Endocrinology 126:2788-2799
    • (1990) Endocrinology , vol.126 , pp. 2788-2799
    • Blithe, D.L.1
  • 41
    • 0001915062 scopus 로고
    • Chemistry of the peptide components of glycoprotein hormones
    • Keel BA, Grotjan Jr HE (eds) CRC Press, Boca Raton
    • Ward DN, Bousfield GR, Gordon WL, Sugino H 1989 Chemistry of the peptide components of glycoprotein hormones. In: Keel BA, Grotjan Jr HE (eds) Microheterogeneity of Glycoprotein Hormones. CRC Press, Boca Raton, pp 1-21
    • (1989) Microheterogeneity of Glycoprotein Hormones , pp. 1-21
    • Ward, D.N.1    Bousfield, G.R.2    Gordon, W.L.3    Sugino, H.4
  • 43
    • 0025355741 scopus 로고
    • Structure determination of the major N- and O-linked carbohydrate chains of the β subunit from equine chorionic gonadotropin
    • Damm JBL, Hard K, Kammerling JP, van Dedem GWK, Vliegenthart FG 1990 Structure determination of the major N- and O-linked carbohydrate chains of the β subunit from equine chorionic gonadotropin. Eur J Biochem 189:175-183
    • (1990) Eur J Biochem , vol.189 , pp. 175-183
    • Damm, J.B.L.1    Hard, K.2    Kammerling, J.P.3    Van Dedem, G.W.K.4    Vliegenthart, F.G.5
  • 45
    • 0024282581 scopus 로고
    • Pituitary glycoprotein hormone oligosaccharides: Structure, synthesis and function of the asparagine-linked oligosaccharides on lutropin, follitropin and thyrotropin
    • Baenziger JU, Green ED 1988 Pituitary glycoprotein hormone oligosaccharides: structure, synthesis and function of the asparagine-linked oligosaccharides on lutropin, follitropin and thyrotropin. Bioch Biophys Acta 947:287-306
    • (1988) Bioch Biophys Acta , vol.947 , pp. 287-306
    • Baenziger, J.U.1    Green, E.D.2
  • 46
    • 0029015130 scopus 로고
    • Separation of asparagine-linked oligosaccharides by high-pH anion-exchange chromatography with pulsed amperometric detection: Empirical relationships between oligosaccharide structure and chromatographic retention
    • Rohrer JS 1995 Separation of asparagine-linked oligosaccharides by high-pH anion-exchange chromatography with pulsed amperometric detection: empirical relationships between oligosaccharide structure and chromatographic retention. Glycobiology 5:359-363
    • (1995) Glycobiology , vol.5 , pp. 359-363
    • Rohrer, J.S.1
  • 47
    • 0022526686 scopus 로고
    • Enzymatic deglycosylation of thryoid-stimulating hormone with peptide N-glycosidase F and endo-β-N-acetylglucosamindase F
    • Lee K-O, Gesundheit N, Chen H-C, Weintraub BD 1986 Enzymatic deglycosylation of thryoid-stimulating hormone with peptide N-glycosidase F and endo-β-N-acetylglucosamindase F. Biochem Biophys Res Commun 138:230-237
    • (1986) Biochem Biophys Res Commun , vol.138 , pp. 230-237
    • Lee, K.-O.1    Gesundheit, N.2    Chen, H.-C.3    Weintraub, B.D.4
  • 48
    • 0023701426 scopus 로고
    • Site-specific mutagenesis defines the intracellular role of the asparagine-linked oligosaccharides of chorionic gonadotropin β subunit
    • Matzuk MM, Boime I 1988 Site-specific mutagenesis defines the intracellular role of the asparagine-linked oligosaccharides of chorionic gonadotropin β subunit. J Biol Chem 263:17106-17111
    • (1988) J Biol Chem , vol.263 , pp. 17106-17111
    • Matzuk, M.M.1    Boime, I.2
  • 49
    • 0028239914 scopus 로고
    • Misfolded human chorionic gonadotropin β subunits are secreted from transfected Chinese hamster ovary cells
    • Bedows E, Norton SH, Huth JR, Suganumea N, Boime I, Ruddon RW 1994 Misfolded human chorionic gonadotropin β subunits are secreted from transfected Chinese hamster ovary cells. J Biol Chem 269:10574-10580
    • (1994) J Biol Chem , vol.269 , pp. 10574-10580
    • Bedows, E.1    Norton, S.H.2    Huth, J.R.3    Suganumea, N.4    Boime, I.5    Ruddon, R.W.6
  • 50
    • 0026793042 scopus 로고
    • The asparagine-linked oligosaccharides at individual glycosylation sites in human thyrotropin
    • Hiyama J, Weisshaar G, Renwick AGC 1992 The asparagine-linked oligosaccharides at individual glycosylation sites in human thyrotropin. Glycobiology 2:401-409
    • (1992) Glycobiology , vol.2 , pp. 401-409
    • Hiyama, J.1    Weisshaar, G.2    Renwick, A.G.C.3
  • 51
    • 0027998433 scopus 로고
    • Evidence for two folding domains in glycoprotein hormone α subunits
    • Bousfield GR, Ward DN 1994 Evidence for two folding domains in glycoprotein hormone α subunits. Endocrinology 135:624-635
    • (1994) Endocrinology , vol.135 , pp. 624-635
    • Bousfield, G.R.1    Ward, D.N.2
  • 52
    • 0027182764 scopus 로고
    • Protein folding and assembly in vitro parallel intracellular folding and assembly: Catalysis of folding and assembly of the human chorionic gonadotropin αβ dimer by protein disulfide isomerase
    • Huth JR, Perini F, Lockridge O, Bedows E, Ruddon RW 1993 Protein folding and assembly in vitro parallel intracellular folding and assembly: catalysis of folding and assembly of the human chorionic gonadotropin αβ dimer by protein disulfide isomerase. J Biol Chem 268:16472-16482
    • (1993) J Biol Chem , vol.268 , pp. 16472-16482
    • Huth, J.R.1    Perini, F.2    Lockridge, O.3    Bedows, E.4    Ruddon, R.W.5
  • 54
    • 0028983425 scopus 로고
    • The lutropin β-subunit N-terminus facilitates subunit combination by offsetting the inhibitory effects of residues needed for LH activity
    • Slaughter S, Wang Y, Myers RV, Moyle WR 1995 The lutropin β-subunit N-terminus facilitates subunit combination by offsetting the inhibitory effects of residues needed for LH activity. Mol Cell Endocrinol 112:21-25
    • (1995) Mol Cell Endocrinol , vol.112 , pp. 21-25
    • Slaughter, S.1    Wang, Y.2    Myers, R.V.3    Moyle, W.R.4
  • 55
    • 0028855750 scopus 로고
    • The role of glcosylation in regulating the glycoprotein hormone free α subunit and free β subunit combination in the extraembryonic coelomic fluid of early pregnancy
    • Blithe DL, Ilies RK 1995 The role of glcosylation in regulating the glycoprotein hormone free α subunit and free β subunit combination in the extraembryonic coelomic fluid of early pregnancy. Endocrinology 136:903-910
    • (1995) Endocrinology , vol.136 , pp. 903-910
    • Blithe, D.L.1    Ilies, R.K.2
  • 56
    • 0016228403 scopus 로고
    • Chemical and biological properties of the subunits of pregnant mare serum gonadotropin
    • Papkoff H 1974 Chemical and biological properties of the subunits of pregnant mare serum gonadotropin. Biochem Biophys Res Commun 58:397-404
    • (1974) Biochem Biophys Res Commun , vol.58 , pp. 397-404
    • Papkoff, H.1
  • 57
    • 0019186369 scopus 로고
    • Pregnant mare serum gomadotropin: An in vitro biological characterization of the lutropin-follitropin dual activity
    • Moore Jr WT, Ward DN 1980 Pregnant mare serum gomadotropin: an in vitro biological characterization of the lutropin-follitropin dual activity. J Biol Chem 255:6930-6936
    • (1980) J Biol Chem , vol.255 , pp. 6930-6936
    • Moore Jr., W.T.1    Ward, D.N.2
  • 58
    • 0021928573 scopus 로고
    • Hybrids from equine LH: Alpha enhances, beta diminishes activity
    • Bousfield GR, Liu W-K, Ward DN 1985 Hybrids from equine LH: alpha enhances, beta diminishes activity. Mol Cell Endocrinol 40: 69-77
    • (1985) Mol Cell Endocrinol , vol.40 , pp. 69-77
    • Bousfield, G.R.1    Liu, W.-K.2    Ward, D.N.3
  • 59
    • 0022492598 scopus 로고
    • Deglycosylated human follitropin: Characterization and effects on adenosine cyclic 3′,5′-phosphate production in porcine granulosa cells
    • Calvo FO, Keutmann HT, Bergert ER, Ryan RJ 1986 Deglycosylated human follitropin: characterization and effects on adenosine cyclic 3′,5′-phosphate production in porcine granulosa cells. Biochemistry 25:3938-3943
    • (1986) Biochemistry , vol.25 , pp. 3938-3943
    • Calvo, F.O.1    Keutmann, H.T.2    Bergert, E.R.3    Ryan, R.J.4
  • 61
    • 0018609789 scopus 로고
    • The binding of FSH, LH, and PMSG to equine gonadal tissues
    • Stewart F, Allen WR 1979 The binding of FSH, LH, and PMSG to equine gonadal tissues. J Reprod Fertil [Suppl] 27:431-440
    • (1979) J Reprod Fertil [Suppl] , vol.27 , pp. 431-440
    • Stewart, F.1    Allen, W.R.2
  • 62
    • 0021690978 scopus 로고
    • Comparison of in vitro follicle-stimulating hormone (FSH) activity of equine gonadotropins (luteinizing hormone, FSH and chorionic gonadotropin) in male and female rats
    • Combarnous Y, Guillou F, Martinat N 1984 Comparison of in vitro follicle-stimulating hormone (FSH) activity of equine gonadotropins (luteinizing hormone, FSH and chorionic gonadotropin) in male and female rats. Endocrinology 115:1821-1827
    • (1984) Endocrinology , vol.115 , pp. 1821-1827
    • Combarnous, Y.1    Guillou, F.2    Martinat, N.3
  • 63
    • 0029931343 scopus 로고    scopus 로고
    • Negative influence of O-linked oligosaccharides of high molecular weight equine chorionic gonadotropin on its luteinizing hormone and follicle-stimulating hormone receptor-binding activities
    • Butnev VY, Gotschall RR, Baker VL, Moore WT, Bousfield GR 1996 Negative influence of O-linked oligosaccharides of high molecular weight equine chorionic gonadotropin on its luteinizing hormone and follicle-stimulating hormone receptor-binding activities. Endocrinology 137:2530-2542
    • (1996) Endocrinology , vol.137 , pp. 2530-2542
    • Butnev, V.Y.1    Gotschall, R.R.2    Baker, V.L.3    Moore, W.T.4    Bousfield, G.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.