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Volumn 94, Issue 10, 2015, Pages 2495-2505

Comparative proteomic analysis of egg white proteins during the rapid embryonic growth period by combinatorial peptide ligand libraries

Author keywords

Combinatorial peptide ligand libraries; Hen egg white; Incubation; Matrix assisted laser desorption ionization time of flight with two mass analyzers for tandem mass spectrometry; Proteomics; Two dimensional gel electrophoresis

Indexed keywords

AVIAN PROTEIN; EGG PROTEIN; PROTEOME;

EID: 84943384216     PISSN: 00325791     EISSN: 15253171     Source Type: Journal    
DOI: 10.3382/ps/pev176     Document Type: Article
Times cited : (25)

References (52)
  • 1
    • 63049100764 scopus 로고    scopus 로고
    • The art of observing rare protein species in proteomes with peptide ligand libraries
    • Boschetti, E., and P. G. Righetti. 2009. The art of observing rare protein species in proteomes with peptide ligand libraries. Proteomics 9:1492-1510.
    • (2009) Proteomics , vol.9 , pp. 1492-1510
    • Boschetti, E.1    Righetti, P.G.2
  • 2
  • 4
    • 0013769948 scopus 로고
    • The mechanism of protein synthesis in the developing chick embryo. The incorporation of free amino acids
    • Carey, N. 1964. The mechanism of protein synthesis in the developing chick embryo. The incorporation of free amino acids. Biochem. J. 91:335-340.
    • (1964) Biochem. J. , vol.91 , pp. 335-340
    • Carey, N.1
  • 7
    • 0034051575 scopus 로고    scopus 로고
    • Effects of ambient temperature on avian incubation behavior
    • Conway, C. J., and T. E. Martin. 2000. Effects of ambient temperature on avian incubation behavior. Behav. Ecol. 11:178-188.
    • (2000) Behav. Ecol. , vol.11 , pp. 178-188
    • Conway, C.J.1    Martin, T.E.2
  • 8
    • 0016087334 scopus 로고
    • Changes in egg white during incubation of the fertile egg
    • Cunningham, F. 1974. Changes in egg white during incubation of the fertile egg. Poult. Sci. 53:1561-1565.
    • (1974) Poult. Sci. , vol.53 , pp. 1561-1565
    • Cunningham, F.1
  • 10
    • 56049096254 scopus 로고    scopus 로고
    • Important metabolic pathways in poultry embryos prior to hatch
    • De Oliveira, J., Z. Uni, and P. Ferket. 2008. Important metabolic pathways in poultry embryos prior to hatch. World's Poult. Sci. J. 64:488-499.
    • (2008) World's Poult. Sci. J. , vol.64 , pp. 488-499
    • De Oliveira, J.1    Uni, Z.2    Ferket, P.3
  • 11
  • 12
    • 0035914376 scopus 로고    scopus 로고
    • Ovocalyxin-32, a novel chicken eggshell matrix protein isolation, amino acid sequencing, cloning, and immunocytochemical localazation
    • Gautron, J., M. T. Hincke, K. Mann, M. Panhéleux, M. Bain, M. D. McKee, S. E. Solomon, and Y. Nys. 2001. Ovocalyxin-32, a novel chicken eggshell matrix protein isolation, amino acid sequencing, cloning, and immunocytochemical localazation. J. Biol. Chem. 276:39243-39252.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39243-39252
    • Gautron, J.1    Hincke, M.T.2    Mann, K.3    Panhéleux, M.4    Bain, M.5    McKee, M.D.6    Solomon, S.E.7    Nys, Y.8
  • 14
    • 0034662907 scopus 로고    scopus 로고
    • Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology
    • Gygi, S. P., G. L. Corthals, Y. Zhang, Y. Rochon, and R. Aebersold. 2000. Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology. Proc. Natl. Acad. Sci. 97:9390-9395.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 9390-9395
    • Gygi, S.P.1    Corthals, G.L.2    Zhang, Y.3    Rochon, Y.4    Aebersold, R.5
  • 15
    • 0024257423 scopus 로고
    • Incubating female passerines do not let the egg temperature fall below the 'physiological zero temperature' during their absences from the nest
    • Haftorn, S. 1988. Incubating female passerines do not let the egg temperature fall below the 'physiological zero temperature' during their absences from the nest. Ornis Scandinavica 19:97-110.
    • (1988) Ornis Scandinavica , vol.19 , pp. 97-110
    • Haftorn, S.1
  • 16
    • 0033822833 scopus 로고    scopus 로고
    • Identification and localization of lysozyme as a component of eggshell membranes and eggshell matrix
    • Hincke, M., J. Gautron, M. Panheleux, J. Garcia-Ruiz, M. McKee, and Y. Nys. 2000. Identification and localization of lysozyme as a component of eggshell membranes and eggshell matrix. Matrix Biol. 19:443-453.
    • (2000) Matrix Biol. , vol.19 , pp. 443-453
    • Hincke, M.1    Gautron, J.2    Panheleux, M.3    Garcia-Ruiz, J.4    McKee, M.5    Nys, Y.6
  • 17
    • 31444451638 scopus 로고    scopus 로고
    • Ovalbuminrelated gene y protein bears carbohydrate chains of the ovomucoid type
    • Hirose, J., Y. Doi, N. Kitabatake, and H. Narita. 2006. Ovalbuminrelated gene Y protein bears carbohydrate chains of the ovomucoid type. Biosci. Biotechnol. Biochem. 70:144-151.
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 144-151
    • Hirose, J.1    Doi, Y.2    Kitabatake, N.3    Narita, H.4
  • 18
    • 84943410495 scopus 로고
    • The change in the concentration of ovoglobulin in egg white during egg formation
    • Hughes, J., and H. Scott. 1936. The change in the concentration of ovoglobulin in egg white during egg formation. Poult. Sci. 15:349-351.
    • (1936) Poult. Sci. , vol.15 , pp. 349-351
    • Hughes, J.1    Scott, H.2
  • 19
    • 77949805991 scopus 로고    scopus 로고
    • Protein?protein interactions in ovalbumin solutions studied by small-angle scattering: Effect of ionic strength and the chemical nature of cations
    • Ianeselli, L., F. Zhang, M. W. Skoda, R. M. Jacobs, R. A. Martin, S. Callow, S. Prévost, and F. Schreiber. 2010. Protein?protein interactions in ovalbumin solutions studied by small-angle scattering: Effect of ionic strength and the chemical nature of cations. J. Phys. Chem. B 114:3776-3783.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 3776-3783
    • Ianeselli, L.1    Zhang, F.2    Skoda, M.W.3    Jacobs, R.M.4    Martin, R.A.5    Callow, S.6    Prévost, S.7    Schreiber, F.8
  • 20
    • 0035970834 scopus 로고    scopus 로고
    • The expression profiles of neurotrophins and their receptors in rat and chicken tissues during development
    • Ip, F. C., J. Cheung, and N. Y. Ip. 2001. The expression profiles of neurotrophins and their receptors in rat and chicken tissues during development. Neurosci. Lett. 301:107-110.
    • (2001) Neurosci. Lett. , vol.301 , pp. 107-110
    • Ip, F.C.1    Cheung, J.2    Ip, N.Y.3
  • 22
    • 0023129864 scopus 로고
    • Chicken ovomucoid: Determination of its amino acid sequence, determination of the trypsin reactive site, and preparation of all three of its domains
    • Kato, I., J. Schrode, W. J. Kohr, and M. Laskowski, Jr. 1987. Chicken ovomucoid: Determination of its amino acid sequence, determination of the trypsin reactive site, and preparation of all three of its domains. Biochemistry 26:193-201.
    • (1987) Biochemistry , vol.26 , pp. 193-201
    • Kato, I.1    Schrode, J.2    Kohr, W.J.3    Laskowski, M.4
  • 23
    • 0033215391 scopus 로고    scopus 로고
    • Crystal Structure of hen apo-ovotransferrin: Both lobes adopt an open conformation upon loss of iron
    • Kurokawa, H., J. C. Dewan, B. Mikami, J. C. Sacchettini, and M. Hirose. 1999. Crystal Structure of hen apo-ovotransferrin: Both lobes adopt an open conformation upon loss of iron. J. Biol. Chem. 274:28445-28452.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28445-28452
    • Kurokawa, H.1    Dewan, J.C.2    Mikami, B.3    Sacchettini, J.C.4    Hirose, M.5
  • 24
    • 34548241810 scopus 로고    scopus 로고
    • Using proteomics to understand avian systems biology and infectious disease
    • Liu, H.-C., and J. Hicks. 2007. Using proteomics to understand avian systems biology and infectious disease. Poult. Sci. 86: 1523-1529.
    • (2007) Poult. Sci. , vol.86 , pp. 1523-1529
    • Liu, H.-C.1    Hicks, J.2
  • 25
    • 84879145097 scopus 로고    scopus 로고
    • Comparative proteomic analysis of hen egg white proteins during early phase of embryonic development by combinatorial peptide ligand library and matrix-assisted laser desorption ionization-time of flight
    • Liu, Y., N. Qiu, and M. Ma. 2013. Comparative proteomic analysis of hen egg white proteins during early phase of embryonic development by combinatorial peptide ligand library and matrix-assisted laser desorption ionization-time of flight. Poult. Sci. 92:1897-1904.
    • (2013) Poult. Sci. , vol.92 , pp. 1897-1904
    • Liu, Y.1    Qiu, N.2    Ma, M.3
  • 26
    • 0033548184 scopus 로고    scopus 로고
    • Multiple involvement of clusterin in chicken ovarian follicle development
    • Mahon, M. G., K. A. Lindstedt, M. Hermann, J. Nimpf, and W. J. Schneider. 1999. Multiple involvement of clusterin in chicken ovarian follicle development. J. Biol. Chem. 274:4036-4044.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4036-4044
    • Mahon, M.G.1    Lindstedt, K.A.2    Hermann, M.3    Nimpf, J.4    Schneider, W.J.5
  • 27
    • 35348963096 scopus 로고    scopus 로고
    • The chicken egg white proteome
    • Mann, K. 2007. The chicken egg white proteome. Proteomics 7:3558-3568.
    • (2007) Proteomics , vol.7 , pp. 3558-3568
    • Mann, K.1
  • 28
    • 46049101500 scopus 로고    scopus 로고
    • Proteomic analysis of the chicken egg vitelline membrane
    • Mann, K. 2008. Proteomic analysis of the chicken egg vitelline membrane. Proteomics 8:2322-2332.
    • (2008) Proteomics , vol.8 , pp. 2322-2332
    • Mann, K.1
  • 29
    • 0242606865 scopus 로고    scopus 로고
    • Disulfide-linked heterodimeric clusterin is a component of the chicken eggshell matrix and egg white
    • Mann, K., J. Gautron, Y. Nys, M. D. McKee, T. Bajari, W. J. Schneider, and M. T. Hincke. 2003. Disulfide-linked heterodimeric clusterin is a component of the chicken eggshell matrix and egg white. Matrix Biol. 22:397-407.
    • (2003) Matrix Biol. , vol.22 , pp. 397-407
    • Mann, K.1    Gautron, J.2    Nys, Y.3    McKee, M.D.4    Bajari, T.5    Schneider, W.J.6    Hincke, M.T.7
  • 30
    • 0022505277 scopus 로고
    • Differential polyadenylation pattern of ovalbumin precursor RNAs during development
    • Messer, R., H. Schröder, H.-J. Breter, and W. Müller. 1986. Differential polyadenylation pattern of ovalbumin precursor RNAs during development. Mol. Biol. Rep. 11:81-86.
    • (1986) Mol. Biol. Rep. , vol.11 , pp. 81-86
    • Messer, R.1    Schröder, H.2    Breter, H.-J.3    Müller, W.4
  • 33
    • 34250192949 scopus 로고    scopus 로고
    • Nutrition of the developing embryo and hatchling
    • Moran, E. 2007. Nutrition of the developing embryo and hatchling. Poult. Sci. 86:1043-1049.
    • (2007) Poult. Sci. , vol.86 , pp. 1043-1049
    • Moran, E.1
  • 34
    • 0037317857 scopus 로고    scopus 로고
    • Cloning and characterization of HEP21, a new member of the uPAR/Ly6 protein superfamily predominantly expressed in hen egg white
    • Nau, F., C. Guerin-Dubiard, C. Desert, J. Gautron, S. Bouton, J. Gribonval, and S. Lagarrigue. 2003. Cloning and characterization of HEP21, a new member of the uPAR/Ly6 protein superfamily predominantly expressed in hen egg white. Poult. Sci. 82:242-250.
    • (2003) Poult. Sci. , vol.82 , pp. 242-250
    • Nau, F.1    Guerin-Dubiard, C.2    Desert, C.3    Gautron, J.4    Bouton, S.5    Gribonval, J.6    Lagarrigue, S.7
  • 36
    • 78650404444 scopus 로고    scopus 로고
    • Proteomic analysis of egg white proteins during storage
    • Omana, D. A., Y. Liang, N. N. Kav, and J. Wu. 2011. Proteomic analysis of egg white proteins during storage. Proteomics 11:144-153.
    • (2011) Proteomics , vol.11 , pp. 144-153
    • Omana, D.A.1    Liang, Y.2    Kav, N.N.3    Wu, J.4
  • 37
    • 82755194846 scopus 로고    scopus 로고
    • Gender differences in apolipoprotein D expression during aging and in Alzheimer disease
    • Ordoñez, C., A. Navarro, C. Pérez, E. Mart?nez, E. del Valle, and J. Tolivia. 2012. Gender differences in apolipoprotein D expression during aging and in Alzheimer disease. Neurobiol. Aging 33:433. e11-20.
    • (2012) Neurobiol. Aging , vol.33 , pp. 433e11-433e20
    • Ordoñez, C.1    Navarro, A.2    Pérez, C.3    Martnez, E.4    Del Valle, E.5    Tolivia, J.6
  • 38
    • 84857659294 scopus 로고    scopus 로고
    • Proteomic analysis of egg white proteins during the early phase of embryonic development
    • Qiu, N., M. Ma, Z. Cai, Y. Jin, X. Huang, Q. Huang, and S. Sun. 2012. Proteomic analysis of egg white proteins during the early phase of embryonic development. J. Proteomics 75:1895-1905.
    • (2012) J. Proteomics , vol.75 , pp. 1895-1905
    • Qiu, N.1    Ma, M.2    Cai, Z.3    Jin, Y.4    Huang, X.5    Huang, Q.6    Sun, S.7
  • 39
    • 84871213945 scopus 로고    scopus 로고
    • Fast separation of hen egg white protein with a phosphorylcholine type zwitterionic ion chromatography stationary phase
    • Qu, Q., X. J. Yu, X. Wu, F. Shi, and L. L. Wang. 2012. Fast separation of hen egg white protein with a phosphorylcholine type zwitterionic ion chromatography stationary phase. Chin. Chem. Lett. 23:1389-1392.
    • (2012) Chin. Chem. Lett. , vol.23 , pp. 1389-1392
    • Qu, Q.1    Yu, X.J.2    Wu, X.3    Shi, F.4    Wang, L.L.5
  • 40
    • 33646548247 scopus 로고    scopus 로고
    • Separation and identification of hen egg protein isoforms using SDS-PAGE and 2D gel electrophoresis with MALDI-TOF mass spectrometry
    • Raikos, V., R. Hansen, L. Campbell, and S. R. Euston. 2006. Separation and identification of hen egg protein isoforms using SDS-PAGE and 2D gel electrophoresis with MALDI-TOF mass spectrometry. Food Chem. 99:702-710.
    • (2006) Food Chem. , vol.99 , pp. 702-710
    • Raikos, V.1    Hansen, R.2    Campbell, L.3    Euston, S.R.4
  • 42
    • 56049095984 scopus 로고    scopus 로고
    • The chicken embryo and its micro environment during egg storage and early incubation
    • Reijrink, I., R. Meijerhof, B. Kemp, and H. van den Brand. 2008. The chicken embryo and its micro environment during egg storage and early incubation. World's Poult. Sci. J. 64:581-598.
    • (2008) World's Poult. Sci. J. , vol.64 , pp. 581-598
    • Reijrink, I.1    Meijerhof, R.2    Kemp, B.3    Brand Den H.Van4
  • 43
    • 32444432614 scopus 로고    scopus 로고
    • Functional analysis of chick ONT1 reveals distinguishable activities among olfactomedinrelated signaling factors
    • Sakuragi, M., N. Sasai, M. Ikeya, M. Kawada, T. Onai, T. Katahira, H. Nakamura, and Y. Sasai. 2006. Functional analysis of chick ONT1 reveals distinguishable activities among olfactomedinrelated signaling factors. Mechanisms Dev. 123:114-123.
    • (2006) Mechanisms Dev. , vol.123 , pp. 114-123
    • Sakuragi, M.1    Sasai, N.2    Ikeya, M.3    Kawada, M.4    Onai, T.5    Katahira, T.6    Nakamura, H.7    Sasai, Y.8
  • 44
    • 14744299061 scopus 로고    scopus 로고
    • Competitive exclusion in poultry-30 years of research
    • Schneitz, C. 2005. Competitive exclusion in poultry-30 years of research. Food Control 16:657-667.
    • (2005) Food Control , vol.16 , pp. 657-667
    • Schneitz, C.1
  • 45
    • 0023664395 scopus 로고
    • Ovoinhibitor introns specify functional domains as in the related and linked ovomucoid gene
    • Scott, M. J., C. Huckaby, I. Kato, W. Kohr, M. Laskowski, Jr, M. Tsai, and B. O'Malley. 1987. Ovoinhibitor introns specify functional domains as in the related and linked ovomucoid gene. J. Biol. Chem. 262:5899-5907.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5899-5907
    • Scott, M.J.1    Huckaby, C.2    Kato, I.3    Kohr, W.4    Laskowski, M.5    Tsai, M.6    O'Malley, B.7
  • 46
    • 0345175676 scopus 로고
    • Peptide mapping of ovoglobulins G2A and G2B in the domestic fowl
    • Stevens, L., and D. Duncan. 1988. Peptide mapping of ovoglobulins G2A and G2B in the domestic fowl. Br. Poult. Sci. 29:665-669.
    • (1988) Br. Poult. Sci. , vol.29 , pp. 665-669
    • Stevens, L.1    Duncan, D.2
  • 47
  • 48
    • 73049100386 scopus 로고    scopus 로고
    • Olfactomedin domaincontaining proteins: Possible mechanisms of action and functions in normal development and pathology
    • Tomarev, S. I., and N. Nakaya. 2009. Olfactomedin domaincontaining proteins: Possible mechanisms of action and functions in normal development and pathology. Mol. Neurobiol. 40:122-138.
    • (2009) Mol. Neurobiol. , vol.40 , pp. 122-138
    • Tomarev, S.I.1    Nakaya, N.2
  • 49
    • 0020064575 scopus 로고
    • The relationship between eggshell porosity and oxygen consumption of the embryo in the domestic fowl
    • Tullett, S., and D. Deeming. 1982. The relationship between eggshell porosity and oxygen consumption of the embryo in the domestic fowl. Compar. Biochem. Physiol. A Physiol. 72:529-533.
    • (1982) Compar. Biochem. Physiol. A Physiol. , vol.72 , pp. 529-533
    • Tullett, S.1    Deeming, D.2
  • 50
    • 0028826645 scopus 로고
    • Identification of a circulatory and oocytic avian apolipoprotein D
    • Vieira, A. V., K. Lindstedt, W. J. Schneider, and P. M. Vieira. 1995. Identification of a circulatory and oocytic avian apolipoprotein D. Mol. Reprod. Dev. 42:443-446.
    • (1995) Mol. Reprod. Dev. , vol.42 , pp. 443-446
    • Vieira, A.V.1    Lindstedt, K.2    Schneider, W.J.3    Vieira, P.M.4
  • 51
    • 84862923501 scopus 로고    scopus 로고
    • Proteomics analysis of egg white proteins from different egg varieties
    • Wang, J., Y. Liang, D. A. Omana, N. N. V. Kav, and J. Wu. 2012. Proteomics analysis of egg white proteins from different egg varieties. J. Agric. Food Chem. 60:272-282.
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 272-282
    • Wang, J.1    Liang, Y.2    Omana, D.A.3    Kav, N.N.V.4    Wu, J.5
  • 52
    • 0031886062 scopus 로고    scopus 로고
    • Identification and characterization of tenp, a gene transiently expressed before overt cell differentiation during neurogenesis
    • Yan, R. T., and S. Z. Wang. 1998. Identification and characterization of tenp, a gene transiently expressed before overt cell differentiation during neurogenesis. J. Neurobiol. 34:319-328.
    • (1998) J. Neurobiol. , vol.34 , pp. 319-328
    • Yan, R.T.1    Wang, S.Z.2


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