메뉴 건너뛰기




Volumn 23, Issue 6, 1998, Pages 689-698

Amino acid sequence, post-translational modifications, binding and labelling of porcine odorant-binding protein

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BINDING PROTEIN; CYSTEINE; LIPOCALIN; POLYPEPTIDE; PYROGLUTAMIC ACID;

EID: 0031701117     PISSN: 0379864X     EISSN: None     Source Type: Journal    
DOI: 10.1093/chemse/23.6.689     Document Type: Article
Times cited : (40)

References (43)
  • 2
    • 0002573969 scopus 로고
    • Molecular mechanism of olfactory signal transduction
    • Corey, D.P. and Roper, S.D. (eds), The Rockefeller University Press, New York
    • Breer H., Boekhoff I., Krieger J., Raming K., Strotmann J. and Tareilus, E. (1992) Molecular mechanism of olfactory signal transduction. In Corey, D.P. and Roper, S.D. (eds), Sensory Transduction. The Rockefeller University Press, New York, pp. 94-108.
    • (1992) Sensory Transduction , pp. 94-108
    • Breer, H.1    Boekhoff, I.2    Krieger, J.3    Raming, K.4    Strotmann, J.5    Tareilus, E.6
  • 3
    • 0020562171 scopus 로고
    • A rapid filtration assay for soluble receptors using polyethylenimine-treated filters
    • Bruns, R.F., Lawson-Wendling, K. and Pugsley, T.A. (1983) A rapid filtration assay for soluble receptors using polyethylenimine-treated filters. Anal. Biochem., 132, 74-81.
    • (1983) Anal. Biochem. , vol.132 , pp. 74-81
    • Bruns, R.F.1    Lawson-Wendling, K.2    Pugsley, T.A.3
  • 4
    • 0025732668 scopus 로고
    • Purification and characterization of two odorant binding proteins from nasal tissue of rabbit and pig
    • Dal Monte, M., Andreini, I., Revoltella, R. and Pelosi, P. (1991) Purification and characterization of two odorant binding proteins from nasal tissue of rabbit and pig. Comp. Biochem. Physiol., 99B, 445-451.
    • (1991) Comp. Biochem. Physiol. , vol.99 B , pp. 445-451
    • Dal Monte, M.1    Andreini, I.2    Revoltella, R.3    Pelosi, P.4
  • 5
    • 0027717569 scopus 로고
    • Binding of selected odorants to bovine and porcine odorant-binding proteins
    • Dal Monte, M., Centini, M., Anselmi, C. and Pelosi, P. (1993) Binding of selected odorants to bovine and porcine odorant-binding proteins. Chem. Senses, 18, 713-721.
    • (1993) Chem. Senses , vol.18 , pp. 713-721
    • Dal Monte, M.1    Centini, M.2    Anselmi, C.3    Pelosi, P.4
  • 6
    • 0026347802 scopus 로고
    • Molecular cloning of putative odorant-binding and odorant-metabolizing proteins
    • Dear, T.N., Campbell, K. and Rabbitts, T.H. (1991) Molecular cloning of putative odorant-binding and odorant-metabolizing proteins. Biochemistry, 30, 10376-10382.
    • (1991) Biochemistry , vol.30 , pp. 10376-10382
    • Dear, T.N.1    Campbell, K.2    Rabbitts, T.H.3
  • 7
    • 0013802167 scopus 로고
    • Immunochemical study of rat urinary proteins, their relation to serum and kidney proteins
    • Dinh, B.L, Tremblay, A. and Dufour, D. (1965) Immunochemical study of rat urinary proteins, their relation to serum and kidney proteins. J. Immunol., 95, 574-582.
    • (1965) J. Immunol. , vol.95 , pp. 574-582
    • Dinh, B.L.1    Tremblay, A.2    Dufour, D.3
  • 8
    • 0001223846 scopus 로고
    • Major urinary protein complex of normal mice: Origin
    • Finlayson, J.S., Asofsky, R., Potter, M. and Runner, C.C. (1965) Major urinary protein complex of normal mice: origin. Science, 149, 981-982.
    • (1965) Science , vol.149 , pp. 981-982
    • Finlayson, J.S.1    Asofsky, R.2    Potter, M.3    Runner, C.C.4
  • 9
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: Structure and function
    • Flower, D.R. (1996) The lipocalin protein family: structure and function. Biochem. J., 318, 1-14.
    • (1996) Biochem. J. , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 10
    • 0030796998 scopus 로고    scopus 로고
    • Microheterogeneity of odorant-binding proteins in the porcupine revealed by N-terminal sequencing and mass spectrometry
    • Ganni M., Garibotti, M., Scaloni, A., Pucci, P. and Pelosi, P. (1997) Microheterogeneity of odorant-binding proteins in the porcupine revealed by N-terminal sequencing and mass spectrometry. Comp. Biochem. Physiol., 117B, 287-291.
    • (1997) Comp. Biochem. Physiol. , vol.117 B , pp. 287-291
    • Ganni, M.1    Garibotti, M.2    Scaloni, A.3    Pucci, P.4    Pelosi, P.5
  • 12
  • 14
    • 0029621033 scopus 로고
    • Affinities of nutty and green-smelling compounds to odorant-binding proteins
    • Hérent, M.F., Collin, S. and Pelosi, P. (1994). Affinities of nutty and green-smelling compounds to odorant-binding proteins. Chem. Senses, 20, 601-610.
    • (1994) Chem. Senses , vol.20 , pp. 601-610
    • Hérent, M.F.1    Collin, S.2    Pelosi, P.3
  • 16
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R.F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol., 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (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
  • 18
    • 0023090806 scopus 로고
    • Isolation of an olfactory cDNA: Similarity to retinol binding protein suggests a role in olfaction
    • Lee, H.K., Wells, R.G. and Reed, R.R. (1987) Isolation of an olfactory cDNA: similarity to retinol binding protein suggests a role in olfaction. Science, 253, 1053-1056.
    • (1987) Science , vol.253 , pp. 1053-1056
    • Lee, H.K.1    Wells, R.G.2    Reed, R.R.3
  • 20
    • 0032521669 scopus 로고    scopus 로고
    • Lipocalins of boar salivary glands binding odours and pheromones
    • Marchese, S., Pes, D., Scaloni, A., Carbone, V. and Pelosi, P. (1998) Lipocalins of boar salivary glands binding odours and pheromones. Eur. J. Biochem., 252, 563-568.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 563-568
    • Marchese, S.1    Pes, D.2    Scaloni, A.3    Carbone, V.4    Pelosi, P.5
  • 21
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsuidara, P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem., 262, 10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsuidara, P.1
  • 22
    • 0028608047 scopus 로고
    • Possible pheromone-carrier function of two lipocalin proteins in the vomeronasal organ
    • Miyawaki, A., Matsushita, F., Ryo, Y. and Mikoshiba, K. (1994) Possible pheromone-carrier function of two lipocalin proteins in the vomeronasal organ. EMBO J., 13, 5835-5842.
    • (1994) EMBO J. , vol.13 , pp. 5835-5842
    • Miyawaki, A.1    Matsushita, F.2    Ryo, Y.3    Mikoshiba, K.4
  • 23
    • 0026715572 scopus 로고
    • Synthesis of thiazole and selenazole derivatives with affinity for the odorant-binding protein
    • Napolitano, E. and Pelosi, P. (1992) Synthesis of thiazole and selenazole derivatives with affinity for the odorant-binding protein. Bioorg. Med. Chem. Lett., 2, 1603-1606.
    • (1992) Bioorg. Med. Chem. Lett. , vol.2 , pp. 1603-1606
    • Napolitano, E.1    Pelosi, P.2
  • 24
    • 0029987549 scopus 로고    scopus 로고
    • Glutamate 1-semialdehyde aminotransferase from Sulfolobus solfataricus
    • Palmieri, G., Di Palo, M., Scaloni, A., Orru', S., Marino, G. and Sannia, G. (1996) Glutamate 1-semialdehyde aminotransferase from Sulfolobus solfataricus. Biochem. J., 320, 541-545.
    • (1996) Biochem. J. , vol.320 , pp. 541-545
    • Palmieri, G.1    Di Palo, M.2    Scaloni, A.3    Orru', S.4    Marino, G.5    Sannia, G.6
  • 26
    • 0029921089 scopus 로고    scopus 로고
    • Perireceptor events in olfaction
    • Pelosi, P. (1996) Perireceptor events in olfaction. J. Neurobiol., 30, 3-19.
    • (1996) J. Neurobiol. , vol.30 , pp. 3-19
    • Pelosi, P.1
  • 27
    • 0025299104 scopus 로고
    • Odorant binding proteins in vertebrates and insects: Similarities and possible common function
    • Pelosi, P. and Maida, R. (1990) Odorant binding proteins in vertebrates and insects: similarities and possible common function. Chem. Senses, 15, 205-215.
    • (1990) Chem. Senses , vol.15 , pp. 205-215
    • Pelosi, P.1    Maida, R.2
  • 28
    • 0000499108 scopus 로고
    • Structure/activity studies and characterization of an odorant-binding protein
    • Brand, J.G., Teeter, J.H., Cagan, R.H. and Kare, M.R. (eds), Marcel Dekker, New York
    • Pelosi, P. and Tirindelli, R. (1989) Structure/activity studies and characterization of an odorant-binding protein. In Brand, J.G., Teeter, J.H., Cagan, R.H. and Kare, M.R. (eds), Chemical Senses. Vol. 1. Receptor Events and Transduction in Taste and Olfaction. Marcel Dekker, New York, pp. 207-226.
    • (1989) Chemical Senses Vol. 1. Receptor Events and Transduction in Taste and Olfaction , vol.1 , pp. 207-226
    • Pelosi, P.1    Tirindelli, R.2
  • 29
    • 0019949965 scopus 로고
    • Identification of a specific olfactory receptor for 2-isobutyl-3-methoxypyrazine
    • Pelosi, P., Baldaccini, N.E. and Pisanelli, A.M. (1982). Identification of a specific olfactory receptor for 2-isobutyl-3-methoxypyrazine. Biochem. J., 201, 245-248.
    • (1982) Biochem. J. , vol.201 , pp. 245-248
    • Pelosi, P.1    Baldaccini, N.E.2    Pisanelli, A.M.3
  • 30
    • 0028858417 scopus 로고
    • Odorant-binding proteins of the mouse
    • Pes, D. and Pelosi, P. (1995). Odorant-binding proteins of the mouse. Comp. Biochem. Physiol., 112B, 471-479.
    • (1995) Comp. Biochem. Physiol. , vol.112 B , pp. 471-479
    • Pes, D.1    Pelosi, P.2
  • 31
    • 0032575116 scopus 로고    scopus 로고
    • Cloning and expression of odorant-binding proteins la and lb from mouse nasal tissue
    • Pes, D., Mameli, M., Andreini, I., Krieger, J., Weber, M., Breer, H. and Pelosi, P. (1998) Cloning and expression of odorant-binding proteins la and lb from mouse nasal tissue. Gene, 212, 49-55.
    • (1998) Gene , vol.212 , pp. 49-55
    • Pes, D.1    Mameli, M.2    Andreini, I.3    Krieger, J.4    Weber, M.5    Breer, H.6    Pelosi, P.7
  • 32
    • 0023741414 scopus 로고
    • Molecular cloning of odorant-binding protein: Member of a ligand carrier family
    • Pevsner, J., Reed, R.R., Feinstein, P.G. and Snyder, S.H. (1988) Molecular cloning of odorant-binding protein: member of a ligand carrier family. Science 241, 336-339.
    • (1988) Science , vol.241 , pp. 336-339
    • Pevsner, J.1    Reed, R.R.2    Feinstein, P.G.3    Snyder, S.H.4
  • 33
    • 0025259871 scopus 로고
    • Odorant-binding protein: Characterization of ligand binding
    • Pevsner, J., Hou, V., Snowman, A.M. and Snyder, S.H. (1990) Odorant-binding protein: characterization of ligand binding. J. Biol. Chem, 265, 6118-6125.
    • (1990) J. Biol. Chem , vol.265 , pp. 6118-6125
    • Pevsner, J.1    Hou, V.2    Snowman, A.M.3    Snyder, S.H.4
  • 34
    • 0026726499 scopus 로고
    • cDNA cloning and sequencing reveals human tear prealbumin to be a member of the lipophilic-ligand carrier protein superfamily
    • Redl, B., Holzfeind, P. and Lottspeich, F. (1992) cDNA cloning and sequencing reveals human tear prealbumin to be a member of the lipophilic-ligand carrier protein superfamily. J. Biol. Chem., 267, 20282-20287.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20282-20287
    • Redl, B.1    Holzfeind, P.2    Lottspeich, F.3
  • 35
    • 0028149038 scopus 로고
    • Structural analysis and classification of lipocalins and related proteins using a profile-search method
    • Sansom C.E., North A.C.T. and Sawyer L. (1994) Structural analysis and classification of lipocalins and related proteins using a profile-search method. Biochim. Biophys. Acta, 1208, 247-255.
    • (1994) Biochim. Biophys. Acta , vol.1208 , pp. 247-255
    • Sansom, C.E.1    North, A.C.T.2    Sawyer, L.3
  • 36
    • 0023472472 scopus 로고
    • Tricine-sodium dodecylsulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. and von Jagow, G. (1987) Tricine-sodium dodecylsulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem., 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 37
    • 0025176792 scopus 로고
    • Possible role for salivary gland protein in taste reception indicated by homology to lipophilic-ligand carrier proteins
    • Schmale, H., Holtgreve-Grez, H. and Christianse, H. (1990) Possible role for salivary gland protein in taste reception indicated by homology to lipophilic-ligand carrier proteins. Nature, 343, 366-369.
    • (1990) Nature , vol.343 , pp. 366-369
    • Schmale, H.1    Holtgreve-Grez, H.2    Christianse, H.3
  • 38
    • 0023133460 scopus 로고
    • Expression of six mouse major urinary protein genes in the mammary, parotid, sublingual, submaxillary and lachrymal glands and in the liver
    • Shahan, K.M., Denaro, M., Gilmartin, M., Shi, Y. and Derman, E. (1987) Expression of six mouse major urinary protein genes in the mammary, parotid, sublingual, submaxillary and lachrymal glands and in the liver. Mol. Cell. Biol., 7, 1947-1954.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1947-1954
    • Shahan, K.M.1    Denaro, M.2    Gilmartin, M.3    Shi, Y.4    Derman, E.5
  • 39
    • 0020532945 scopus 로고
    • The gene family for major urinary proteins, expression in several secretory tissues of the mouse
    • Shaw, P.H., Held, W.A. and Hastie, N.D. (1983) The gene family for major urinary proteins, expression in several secretory tissues of the mouse. Cell, 32, 755-761.
    • (1983) Cell , vol.32 , pp. 755-761
    • Shaw, P.H.1    Held, W.A.2    Hastie, N.D.3
  • 40
    • 0029760325 scopus 로고    scopus 로고
    • Domain swapping creates a third putative combining site in bovine odorant binding protein dimer
    • Tegoni, M., Ramoni, R., Bignetti, E., Spinelli, S. and Cambillau, C. (1996) Domain swapping creates a third putative combining site in bovine odorant binding protein dimer. Nature Struct. Biol., 3, 863-867.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 863-867
    • Tegoni, M.1    Ramoni, R.2    Bignetti, E.3    Spinelli, S.4    Cambillau, C.5
  • 42
    • 0019489601 scopus 로고
    • Pheromone binding and inactivation by moth antennae
    • Vogt R.G. and Riddiford L.M. (1981) Pheromone binding and inactivation by moth antennae. Nature, 293, 161-163.
    • (1981) Nature , vol.293 , pp. 161-163
    • Vogt, R.G.1    Riddiford, L.M.2
  • 43
    • 0002390695 scopus 로고
    • The biochemistry of odorant reception and transduction
    • Schild, D. (ed.), NATO ASI Series H, Springer-Verlag, Berlin
    • Vogt R.G., Rybczynski R. and Lerner M.R. (1990) The biochemistry of odorant reception and transduction. In Schild, D. (ed.), NATO ASI Series H, Vol. 39, Chemosensory Information Processing. Springer-Verlag, Berlin, pp. 33-76.
    • (1990) Chemosensory Information Processing , vol.39 , pp. 33-76
    • Vogt, R.G.1    Rybczynski, R.2    Lerner, M.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.