메뉴 건너뛰기




Volumn 58, Issue 2, 1998, Pages 458-469

Hormone-specific inhibitory influence of α-subunit Asn56 oligosaccharide on in vitro subunit association and follicle-stimulating hormone receptor binding of equine gonadotropins

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; CARBOHYDRATE; FOLLITROPIN; FOLLITROPIN RECEPTOR; HYBRID PROTEIN; LUTEINIZING HORMONE; OLIGOSACCHARIDE; PROGESTERONE; SERIC GONADOTROPIN;

EID: 0031933747     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod58.2.458     Document Type: Article
Times cited : (23)

References (66)
  • 1
    • 0000676471 scopus 로고
    • Gonadotropins: Chemistry and biosynthesis
    • Knobil E, Neill JD (eds.), New York: Raven Press
    • Bousfield GR, Perry WM, Ward DN. Gonadotropins: chemistry and biosynthesis. In: Knobil E, Neill JD (eds.), The Physiology of Reproduction. New York: Raven Press; 1994: 1749-1792.
    • (1994) The Physiology of Reproduction , pp. 1749-1792
    • Bousfield, G.R.1    Perry, W.M.2    Ward, D.N.3
  • 3
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6 O resolution from MAD analysis of the selenomethionyl protein
    • Wu H, Lustbader JW, Liu Y, Canfield RE, Hendrickson WA. Structure of human chorionic gonadotropin at 2.6 O resolution from MAD analysis of the selenomethionyl protein. Structure 1994; 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
  • 5
    • 0030037083 scopus 로고    scopus 로고
    • Protein folding in the endoplasmic reticulum: Lessons from the human chorionic gonadotropin β subunit
    • Ruddon RW, Sherman SA, Bedows E. Protein folding in the endoplasmic reticulum: lessons from the human chorionic gonadotropin β subunit. Protein Sci 1996; 5:1443-1452.
    • (1996) Protein Sci , vol.5 , pp. 1443-1452
    • Ruddon, R.W.1    Sherman, S.A.2    Bedows, E.3
  • 6
    • 0029882185 scopus 로고    scopus 로고
    • Long loop residues 33-58 in the human glycoprotein hormone common α subunit contain structural components for subunit heterodimerization and human follitropin-receptor binding
    • Liu C, Dias JA. Long loop residues 33-58 in the human glycoprotein hormone common α subunit contain structural components for subunit heterodimerization and human follitropin-receptor binding. Arch Biochem Biophys 1996; 329:127-135.
    • (1996) Arch Biochem Biophys , vol.329 , pp. 127-135
    • Liu, C.1    Dias, J.A.2
  • 7
    • 0030013815 scopus 로고    scopus 로고
    • Site-directed mutagenesis of amino acids 33-44 of the common α-subunit reveals different structural requirements for heterodimer expression among the glycoprotein hormones and suggests that cyclic adenosine 3′,5′-monophosphate production and growth promotion are potentially dissociable functions of human thyrotropin
    • Grossmann M, Szkudlinski MW, Dias JA, Xia H, Wong R, Puett D, Weintraub BD. Site-directed mutagenesis of amino acids 33-44 of the common α-subunit reveals different structural requirements for heterodimer expression among the glycoprotein hormones and suggests that cyclic adenosine 3′,5′-monophosphate production and growth promotion are potentially dissociable functions of human thyrotropin. Mol Endocrinol 1996; 10:769-779.
    • (1996) Mol Endocrinol , vol.10 , pp. 769-779
    • Grossmann, M.1    Szkudlinski, M.W.2    Dias, J.A.3    Xia, H.4    Wong, R.5    Puett, D.6    Weintraub, B.D.7
  • 8
    • 0028890259 scopus 로고
    • Glycoprotein hormones: Glycobiology of gonadotrophins, thyrotrophin and free α subunit
    • Thotakura NR, Blithe DL. Glycoprotein hormones: glycobiology of gonadotrophins, thyrotrophin and free α subunit. Glycobiology 1995; 5:3-10.
    • (1995) Glycobiology , vol.5 , pp. 3-10
    • Thotakura, N.R.1    Blithe, D.L.2
  • 9
    • 0030596139 scopus 로고    scopus 로고
    • Human follitropin heterodimerization and receptor binding structural motifs: Identification and analysis by a combination of synthetic peptide and mutagenesis approaches
    • Dias JA. Human follitropin heterodimerization and receptor binding structural motifs: identification and analysis by a combination of synthetic peptide and mutagenesis approaches. Mol Cell Endocrinol 1996; 125:45-54.
    • (1996) Mol Cell Endocrinol , vol.125 , pp. 45-54
    • Dias, J.A.1
  • 11
    • 0020161160 scopus 로고
    • α-Subunit conformation in glycoprotein hormones and recombinants as assessed by specific antisera
    • Strickland TW, Puett D. α-Subunit conformation in glycoprotein hormones and recombinants as assessed by specific antisera. Endocrinology 1982; 111:95-100.
    • (1982) Endocrinology , vol.111 , pp. 95-100
    • Strickland, T.W.1    Puett, D.2
  • 12
    • 0019767408 scopus 로고
    • Characteristics of hybrids of ovine LH and human glycoprotein hormone subunits in rat and chicken in vitro test systems
    • Glenn SD, Liu W-K, Ward DN. Characteristics of hybrids of ovine LH and human glycoprotein hormone subunits in rat and chicken in vitro test systems. Biol Reprod 1981; 25:1027-1033.
    • (1981) Biol Reprod , vol.25 , pp. 1027-1033
    • Glenn, S.D.1    Liu, W.-K.2    Ward, D.N.3
  • 13
    • 0021928573 scopus 로고
    • Hybrids from equine LH: Alpha enhances, beta diminishes activity
    • Bousfield GR, Liu W-K, Ward DN. Hybrids from equine LH: alpha enhances, beta diminishes activity. Mol Cell Endocrinol 1985; 40:69-77.
    • (1985) Mol Cell Endocrinol , vol.40 , pp. 69-77
    • Bousfield, G.R.1    Liu, W.-K.2    Ward, D.N.3
  • 14
    • 0026485387 scopus 로고
    • Molecular structures of glycoprotein hormones and functions of their carbohydrate components
    • Hartree A, Renwick AGC. Molecular structures of glycoprotein hormones and functions of their carbohydrate components. Biochem J 1992; 287:665-679.
    • (1992) Biochem J , vol.287 , pp. 665-679
    • Hartree, A.1    Renwick, A.G.C.2
  • 16
    • 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. Specific roles for the asparagine-linked carbohydrate residues of recombinant human follicle stimulating hormone in receptor binding and signal transduction. J Mol Endocrinol 1994; 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
  • 17
    • 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. Site-directed mutagenesis defines the individual roles of the glycosylation sites on follicle-stimulating hormone. J Biol Chem 1994; 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
  • 18
    • 0028006709 scopus 로고
    • Receptor binding and signal transduction are dissociable functions requiring different sites on follicle stimulating hormone
    • Valove FM, Finch C, Anasti JN, Froehlich J, Flack MR. Receptor binding and signal transduction are dissociable functions requiring different sites on follicle stimulating hormone. Endocrinology 1994; 135: 2657-2661.
    • (1994) Endocrinology , vol.135 , pp. 2657-2661
    • Valove, F.M.1    Finch, C.2    Anasti, J.N.3    Froehlich, J.4    Flack, M.R.5
  • 19
    • 0029931343 scopus 로고    scopus 로고
    • Negative influence of O-linked oligosaccharides of high molecular weight equine chorionic gonadotropin (eCG) on its LH anf FSH receptor binding activities
    • Butnev VY, Gotschall RR, Baker VL, Moore WT, Bousfield GR. Negative influence of O-linked oligosaccharides of high molecular weight equine chorionic gonadotropin (eCG) on its LH anf FSH receptor binding activities. Endocrinology 1996; 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
  • 20
    • 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. Pregnant mare serum gonadotropin: rapid isolation procedures for the purification of intact hormone and isolation of subunits. J Biol Chem 1980; 255:6923-6929.
    • (1980) J Biol Chem , vol.255 , pp. 6923-6929
    • Moore Jr., W.T.1    Ward, D.N.2
  • 21
    • 0021353964 scopus 로고
    • Purification of lutropin and follitropin in high yield from horse pituitary glands
    • Bousfield GR, Ward DN. Purification of lutropin and follitropin in high yield from horse pituitary glands. J Biol Chem 1984; 259:1911-1921.
    • (1984) J Biol Chem , vol.259 , pp. 1911-1921
    • Bousfield, G.R.1    Ward, D.N.2
  • 22
    • 84875463071 scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers
    • Hillenkamp F, Karas M, Beavis RC, Chait BT. Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers. Anal Chem 1991; 63:1193A-1203A.
    • (1991) Anal Chem , vol.63
    • Hillenkamp, F.1    Karas, M.2    Beavis, R.C.3    Chait, B.T.4
  • 23
    • 0024498370 scopus 로고
    • Effects of removal of carboxyterminal extension from equine luteinizing hormone (LH) β-subunit on LH and follicle-stimulating hormone receptor binding activities and LH steroidogenic activity in rat testicular Leydig cells
    • Bousfield GR, Liu W-K, Ward DN. Effects of removal of carboxyterminal extension from equine luteinizing hormone (LH) β-subunit on LH and follicle-stimulating hormone receptor binding activities and LH steroidogenic activity in rat testicular Leydig cells. Endocrinology 1989; 124:379-387.
    • (1989) Endocrinology , vol.124 , pp. 379-387
    • Bousfield, G.R.1    Liu, W.-K.2    Ward, D.N.3
  • 24
    • 0022408484 scopus 로고
    • Demonstration of a COOH-terminal extension on equine lutropin by means of a common acid-labile bond in equine lutropin and equine chorionic gonadotropin
    • Bousfield GR, Sugino H, Ward DN. Demonstration of a COOH-terminal extension on equine lutropin by means of a common acid-labile bond in equine lutropin and equine chorionic gonadotropin. J Biol Chem 1985; 260:9531-9533.
    • (1985) J Biol Chem , vol.260 , pp. 9531-9533
    • Bousfield, G.R.1    Sugino, H.2    Ward, D.N.3
  • 25
    • 0028883286 scopus 로고
    • Identification of the sites of N-linked glycosylation on the follicle-stimulating hormone (FSH) receptor and assessment of their role in FSH receptor function
    • Davis D, Liu X, Segaloff DL. Identification of the sites of N-linked glycosylation on the follicle-stimulating hormone (FSH) receptor and assessment of their role in FSH receptor function. Mol Endocrinol 1995; 9:159-170.
    • (1995) Mol Endocrinol , vol.9 , pp. 159-170
    • Davis, D.1    Liu, X.2    Segaloff, D.L.3
  • 28
    • 0018001339 scopus 로고
    • Simultaneous analysis of families of sigmoidal curves: Application to bioassay, radioligand assay, and physiological dose-response curves
    • DeLean A, Munson PJ, Rodbard D. Simultaneous analysis of families of sigmoidal curves: application to bioassay, radioligand assay, and physiological dose-response curves. Am J Physiol 1978; 235:E97-102.
    • (1978) Am J Physiol , vol.235
    • DeLean, A.1    Munson, P.J.2    Rodbard, D.3
  • 29
    • 0021869079 scopus 로고
    • Priming procedure and hormone preparations influence rat granulosa cell response
    • Liu W-K, Bousfield GR, Moore WT Jr, Ward DN. Priming procedure and hormone preparations influence rat granulosa cell response. Endocrinology 1985; 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
  • 31
    • 0017683799 scopus 로고
    • The role of estrogen in the regulation of luteal progesterone secretion in the rat after day 12 of pregnancy
    • Gibori G, Antczak E, Rothchild I. The role of estrogen in the regulation of luteal progesterone secretion in the rat after day 12 of pregnancy. Endocrinology 1977; 100:1483-1495.
    • (1977) Endocrinology , vol.100 , pp. 1483-1495
    • Gibori, G.1    Antczak, E.2    Rothchild, I.3
  • 33
    • 0024340857 scopus 로고
    • Role of carbohydrates in glycoprotein hormone signal transduction
    • Sairam MR. Role of carbohydrates in glycoprotein hormone signal transduction. FASEB J 1989; 3:1915-1926.
    • (1989) FASEB J , vol.3 , pp. 1915-1926
    • Sairam, M.R.1
  • 34
    • 0024511030 scopus 로고
    • Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction
    • Matzuk MM, Keene JL, Boime I. Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction. J Biol Chem 1989; 264:2409-2414.
    • (1989) J Biol Chem , vol.264 , pp. 2409-2414
    • Matzuk, M.M.1    Keene, J.L.2    Boime, I.3
  • 35
    • 0025992391 scopus 로고
    • Site-specific N-glycosylation of human chorionic gonadotropin - Structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy
    • Weisshaar G, Hiyama J, Renwick AGC. Site-specific N-glycosylation of human chorionic gonadotropin - structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy. Glycobiology 1991; 1:393-404.
    • (1991) Glycobiology , vol.1 , pp. 393-404
    • Weisshaar, G.1    Hiyama, J.2    Renwick, A.G.C.3
  • 36
    • 0024991081 scopus 로고
    • Site-specific N-glycosylation of ovine lutropin: Structural analysis by one- and two-dimensional 1H-NMR spectroscopy
    • Weisshaar G, Hiyama J, Renwick AGC. Site-specific N-glycosylation of ovine lutropin: structural analysis by one- and two-dimensional 1H-NMR spectroscopy. Eur J Biochem 1990; 192:741-751.
    • (1990) Eur J Biochem , vol.192 , pp. 741-751
    • Weisshaar, G.1    Hiyama, J.2    Renwick, A.G.C.3
  • 37
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R, Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 1985; 54:631-634.
    • (1985) Annu Rev Biochem , vol.54 , pp. 631-634
    • Kornfeld, R.1    Kornfeld, S.2
  • 39
    • 0021739703 scopus 로고
    • A kinetic comparison of the processing and secretion of the αβ dimer and the uncombined α and β subunits of chorionic gonadotropin synthesized by human choriocarcinoma cells
    • Peters BP, Krzesicki RF, Hartle RJ, Perini F, Ruddon RW. A kinetic comparison of the processing and secretion of the αβ dimer and the uncombined α and β subunits of chorionic gonadotropin synthesized by human choriocarcinoma cells. J Biol Chem 1984; 259:15123-15130.
    • (1984) J Biol Chem , vol.259 , pp. 15123-15130
    • Peters, B.P.1    Krzesicki, R.F.2    Hartle, R.J.3    Perini, F.4    Ruddon, R.W.5
  • 41
    • 0008924615 scopus 로고
    • Gonadotropins: Chemistry and biosynthesis
    • Knobil E, Neill J (eds.), New York: Raven Press, Ltd.
    • Pierce JG. Gonadotropins: chemistry and biosynthesis. In: Knobil E, Neill J (eds.), The Physiology of Reproduction. New York: Raven Press, Ltd.; 1988: 1335-1348.
    • (1988) The Physiology of Reproduction , pp. 1335-1348
    • Pierce, J.G.1
  • 43
    • 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. 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 1993; 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
  • 44
    • 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. The lutropin β-subunit N-terminus facilitates subunit combination by offsetting the inhibitory effects of residues needed for LH activity. Mol Cell Endocrinol 1995; 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
  • 45
    • 0020696020 scopus 로고
    • Purification of an alternate form of the α subunit of the glycoprotein hormones from bovine pituitaries and identification of its O-linked oligosaccharide
    • Parsons TF, Bloomfield GA, Pierce JG. Purification of an alternate form of the α subunit of the glycoprotein hormones from bovine pituitaries and identification of its O-linked oligosaccharide. J Biol Chem 1983; 258:240-244.
    • (1983) J Biol Chem , vol.258 , pp. 240-244
    • Parsons, T.F.1    Bloomfield, G.A.2    Pierce, J.G.3
  • 46
    • 0021342965 scopus 로고
    • Free α-like material from bovine pituitaries: Removal of its O-linked oligosaccharide permits combination with lutropin-β
    • Parsons TF, Pierce JG. Free α-like material from bovine pituitaries: removal of its O-linked oligosaccharide permits combination with lutropin-β. J Biol Chem 1984; 259:2662-2666.
    • (1984) J Biol Chem , vol.259 , pp. 2662-2666
    • Parsons, T.F.1    Pierce, J.G.2
  • 47
    • 0028855750 scopus 로고
    • The role of glycosylation in regulating the glycoprotein hormone free α subunit and free β subunit combination in the extraembryonic coelomic fluid of early pregnancy
    • Blithe DL, Iles RK. The role of glycosylation in regulating the glycoprotein hormone free α subunit and free β subunit combination in the extraembryonic coelomic fluid of early pregnancy. Endocrinology 1995; 136:903-910.
    • (1995) Endocrinology , vol.136 , pp. 903-910
    • Blithe, D.L.1    Iles, R.K.2
  • 48
    • 0025689177 scopus 로고
    • N-Linked oligosaccharides on free α interfere with its ability to combine with human chorionic gonadotropin-β subunit
    • Blithe DL. N-Linked oligosaccharides on free α interfere with its ability to combine with human chorionic gonadotropin-β subunit. J Biol Chem 1990; 265:21951-21956.
    • (1990) J Biol Chem , vol.265 , pp. 21951-21956
    • Blithe, D.L.1
  • 49
    • 0025280694 scopus 로고
    • Carbohydrate composition of the α-subunit of human choriogonadotropin (hCGα) and the free α molecules produced in pregnancy: Most free α and some combined hCGα molecules are fucosylated
    • Blithe DL. Carbohydrate composition of the α-subunit of human choriogonadotropin (hCGα) and the free α molecules produced in pregnancy: most free α and some combined hCGα molecules are fucosylated. Endocrinology 1990; 126:2788-2799.
    • (1990) Endocrinology , vol.126 , pp. 2788-2799
    • Blithe, D.L.1
  • 51
    • 0022258720 scopus 로고
    • A role for glycosylation of the α subunit in transduction of biological signal in glycoprotein hormones
    • Sairam MR, Bhargavi GN. A role for glycosylation of the α subunit in transduction of biological signal in glycoprotein hormones. Science 1985; 229:65-67.
    • (1985) Science , vol.229 , pp. 65-67
    • Sairam, M.R.1    Bhargavi, G.N.2
  • 52
    • 0026458351 scopus 로고
    • Assaying glycoprotein hormones - The influence of glycosylation on immunoreactivity
    • Storring PL. Assaying glycoprotein hormones - the influence of glycosylation on immunoreactivity. Trends Biotechnol 1992; 10:427-432.
    • (1992) Trends Biotechnol , vol.10 , pp. 427-432
    • Storring, P.L.1
  • 53
    • 0021797504 scopus 로고
    • Evidence for a conformational change in deglycosylated glycoprotein hormones
    • Keutmann HT, Johnson L, Ryan RJ. Evidence for a conformational change in deglycosylated glycoprotein hormones. FEBS Lett 1985; 185:333-338.
    • (1985) FEBS Lett , vol.185 , pp. 333-338
    • Keutmann, H.T.1    Johnson, L.2    Ryan, R.J.3
  • 54
    • 0029824825 scopus 로고    scopus 로고
    • NMR studies of the free α subunit of human chorionic gonadotropin: Structural influences of N-glycosylation and the β subunit on the conformation of the α subunit
    • De Beer T, Van Zuylen CWEM, Leeflang BR, Hard K, Boelens R, Kaptein R, Kamerling JP, Viegenthart JFG. NMR studies of the free α subunit of human chorionic gonadotropin: structural influences of N-glycosylation and the β subunit on the conformation of the α subunit. Eur J Biochem 1996; 241:229-242.
    • (1996) Eur J Biochem , vol.241 , pp. 229-242
    • De Beer, T.1    Van Zuylen, C.W.E.M.2    Leeflang, B.R.3    Hard, K.4    Boelens, R.5    Kaptein, R.6    Kamerling, J.P.7    Viegenthart, J.F.G.8
  • 56
    • 0020323244 scopus 로고
    • Biochemical, biological, and immunological properties of chemically deglycosylated human choriogonadotropin
    • Manjunath P, Sairam MR. Biochemical, biological, and immunological properties of chemically deglycosylated human choriogonadotropin. J Biol Chem 1982; 257:7109-7115.
    • (1982) J Biol Chem , vol.257 , pp. 7109-7115
    • Manjunath, P.1    Sairam, M.R.2
  • 58
    • 0001442921 scopus 로고
    • Comparative study of mammalian glycoprotein hormones
    • Alexander NJ (ed.), Baltimore: Harper and Row
    • Ward DN, Moore WT Jr. Comparative study of mammalian glycoprotein hormones. In: Alexander NJ (ed.), Animal Models for Research in Fertility and Contraception. Baltimore: Harper and Row; 1979: 151-164.
    • (1979) Animal Models for Research in Fertility and Contraception , pp. 151-164
    • Ward, D.N.1    Moore Jr., W.T.2
  • 59
  • 60
    • 0018828236 scopus 로고
    • Interaction of equine luteinizing hormone with binding sites for follicle-stimulating hormone in the rat seminiferous tubule
    • Aggarwal BB, Licht P, Papkoff H, Bona-Gallo A. Interaction of equine luteinizing hormone with binding sites for follicle-stimulating hormone in the rat seminiferous tubule. Endocrinology 1980; 107: 725-731.
    • (1980) Endocrinology , vol.107 , pp. 725-731
    • Aggarwal, B.B.1    Licht, P.2    Papkoff, H.3    Bona-Gallo, A.4
  • 61
    • 0019974781 scopus 로고
    • Equine luteinizing hormone possesses follicle-stimulating hormone activity in hypophysectomized female rats
    • Moudgal NR, Papkoff H. Equine luteinizing hormone possesses follicle-stimulating hormone activity in hypophysectomized female rats. Biol Reprod 1982; 26:935-942.
    • (1982) Biol Reprod , vol.26 , pp. 935-942
    • Moudgal, N.R.1    Papkoff, H.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. Comparison of in vitro follicle-stimulating hormone (FSH) activity of equine gonadotropins (luteinizing hormone, FSH and chorionic gonadotropin) in male and female rats. Endocrinology 1984; 115:1821-1827.
    • (1984) Endocrinology , vol.115 , pp. 1821-1827
    • Combarnous, Y.1    Guillou, F.2    Martinat, N.3
  • 63
    • 0022543079 scopus 로고
    • Direct demonstration of intrinsic follicle-stimulating hormone receptor-binding activity in acid-treated equine luteinizing hormone
    • Bousfield GR, Ward DN. Direct demonstration of intrinsic follicle-stimulating hormone receptor-binding activity in acid-treated equine luteinizing hormone. Biochim Biophys Acta 1986; 885:327-334.
    • (1986) Biochim Biophys Acta , vol.885 , pp. 327-334
    • Bousfield, G.R.1    Ward, D.N.2
  • 64
    • 0026099739 scopus 로고
    • Equine chorionic gonadotropin
    • Murphy BD, Martinuk SD. Equine chorionic gonadotropin. Endocr Rev 1991; 12:27-44.
    • (1991) Endocr Rev , vol.12 , pp. 27-44
    • Murphy, B.D.1    Martinuk, S.D.2
  • 65
    • 0022969822 scopus 로고
    • Properties of equine luteinizing hormone alpha subunit alone and in combination with various subunits
    • Roser JF, Carrick FN, Papkoff H. Properties of equine luteinizing hormone alpha subunit alone and in combination with various subunits. Biol Reprod 1986; 35:493-500.
    • (1986) Biol Reprod , vol.35 , pp. 493-500
    • Roser, J.F.1    Carrick, F.N.2    Papkoff, H.3
  • 66
    • 0023760340 scopus 로고
    • Superovulation of immature rats by continuous infusion of follicle-stimulating hormone
    • Armstrong DT, Opavsky MA. Superovulation of immature rats by continuous infusion of follicle-stimulating hormone. Biol Reprod 1988; 39:511-518.
    • (1988) Biol Reprod , vol.39 , pp. 511-518
    • Armstrong, D.T.1    Opavsky, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.