Purificación de IgY contra la subunidad nr3 del receptor nmda de cerebro de rata

Autores:
Méndez, Gina
Reyes, Edgar
Poutou, Raúl
Quevedo, Balkys
Lareo, Leonardo
Tipo de recurso:
Article of journal
Fecha de publicación:
2008
Institución:
Universidad de Córdoba
Repositorio:
Repositorio Institucional Unicórdoba
Idioma:
spa
OAI Identifier:
oai:repositorio.unicordoba.edu.co:ucordoba/5628
Acceso en línea:
https://repositorio.unicordoba.edu.co/handle/ucordoba/5628
https://doi.org/10.21897/rmvz.407
Palabra clave:
NR3 subunit
NMDA receptor
IgY
rat
brain.
Rights
openAccess
License
https://creativecommons.org/licenses/by-nc-sa/4.0/
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oai_identifier_str oai:repositorio.unicordoba.edu.co:ucordoba/5628
network_acronym_str UCORDOBA2
network_name_str Repositorio Institucional Unicórdoba
repository_id_str
dc.title.spa.fl_str_mv Purificación de IgY contra la subunidad nr3 del receptor nmda de cerebro de rata
dc.title.translated.eng.fl_str_mv Purificación de IgY contra la subunidad nr3 del receptor nmda de cerebro de rata
title Purificación de IgY contra la subunidad nr3 del receptor nmda de cerebro de rata
spellingShingle Purificación de IgY contra la subunidad nr3 del receptor nmda de cerebro de rata
NR3 subunit
NMDA receptor
IgY
rat
brain.
title_short Purificación de IgY contra la subunidad nr3 del receptor nmda de cerebro de rata
title_full Purificación de IgY contra la subunidad nr3 del receptor nmda de cerebro de rata
title_fullStr Purificación de IgY contra la subunidad nr3 del receptor nmda de cerebro de rata
title_full_unstemmed Purificación de IgY contra la subunidad nr3 del receptor nmda de cerebro de rata
title_sort Purificación de IgY contra la subunidad nr3 del receptor nmda de cerebro de rata
dc.creator.fl_str_mv Méndez, Gina
Reyes, Edgar
Poutou, Raúl
Quevedo, Balkys
Lareo, Leonardo
dc.contributor.author.spa.fl_str_mv Méndez, Gina
Reyes, Edgar
Poutou, Raúl
Quevedo, Balkys
Lareo, Leonardo
dc.subject.spa.fl_str_mv NR3 subunit
NMDA receptor
IgY
rat
brain.
topic NR3 subunit
NMDA receptor
IgY
rat
brain.
publishDate 2008
dc.date.accessioned.none.fl_str_mv 2008-01-01 00:00:00
2022-07-01T20:59:28Z
dc.date.available.none.fl_str_mv 2008-01-01 00:00:00
2022-07-01T20:59:28Z
dc.date.issued.none.fl_str_mv 2008-01-01
dc.type.spa.fl_str_mv Artículo de revista
dc.type.eng.fl_str_mv Journal article
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dc.type.driver.spa.fl_str_mv info:eu-repo/semantics/article
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dc.identifier.doi.none.fl_str_mv 10.21897/rmvz.407
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url https://repositorio.unicordoba.edu.co/handle/ucordoba/5628
https://doi.org/10.21897/rmvz.407
dc.language.iso.spa.fl_str_mv spa
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dc.relation.references.spa.fl_str_mv 1 Dingledine R, Borges K, Bowie D, Traynelis S. The glutamate receptor ion channels. Pharmacol Rev 1999; 51: 7-61.
2 Pérez I, Schulteis C, Contractor A, Lipton S, Trimmer J, Sucher N, et al. Assembly with the NR1 subunit is required for surface expression or NR3A-containing NMDA Receptors. J Neur 1999; 21: 1228- 1237.
3 Cibarra S, Gahn L, Pecht G, Heinemann S, Sevarino K. Cloning and characterization of chi-1: A developmentally regulated member of a novel class of the ionotropic glutamate receptor family. J Neur 1995; 15: 6498-6508.
4 Sucher N, Akbarian S, Chi C, Leclerc C, Awobuluyi M, Deitcher D, et al. Developmental and regional expression pattern of a novel NMDA receptor-like subunit (NMDAR-L) in the rodent brain. J Neur 1995; 15: 6509-6520.
5 Das S, Sasaki Y, Rothe T, Premkumar L, Takasu M, Crandall J, et al. Increased NMDA current and spine density in mice lacking the NMDA receptor subunit NR3A. Nature 1998; 393: 377-381. http://dx.doi.org/10.1038/30748
6 Sun L, Margolis F, Shipley M, Lidow M. Identification of a long variant of mRNA encoding the NR3 subunit of the NMDA receptor: its regional distribution and developmental expression in the rat brain. FEBS Let 1998; 441: 392-396. http://dx.doi.org/10.1016/S0014-5793(98)01590-7
7 Nishi M, Heather H, Hai-Ping L, Mitsihiru K, Yasunori H. Motoneuron specific expression of NR3B, a novel NMDA type glutamate receptor subunit that works in a dominant negative manner. J Neur 2001; 21: 1-6.
8 Madden D. The structure and function of glutamate receptor ion channels. Nature 2002; 3: 91-101.
9 Morrison S, Mohammed M, Wims L, Trinh R, Etches R. Sequences in antibody molecules important for receptor mediated transport into the chicken egg yolk. Mol Immunol 2001; 38: 619-625. http://dx.doi.org/10.1016/S0161-5890(01)00095-5
10 Patterson R, Youngner J, Weigle W, Dixon F. Antibody production and transfer to egg yolk in chickens. J Inmunol 1962; 89: 272-278.
11 Warr G, Magor K, Higgins D. IgY: clues to the origins if modern antibodies. Immunol Today 1995; 16: 392-398. http://dx.doi.org/10.1016/0167-5699(95)80008-5
12 Narat M. Production of antibodies in chickens. Food Technol Biotechnol 2003; 41: 259-267.
13 IBCP. Pôle BioInformatique Lyonnais, Clustal W PBIL. URL disponible http:// npsa-pbil.ibcp.fr/cgi-bin/ npsa_automat.pl?page=/NPSA/ npsa_clustalw.html. 14 Caprino L, Han G. The 9- fluorenylmethoxycarbonyl group. J Org Chem 1972; 37: 3404-3409. http://dx.doi.org/10.1021/jo00795a005
15 Merrifield R. Solid phase peptide synthesis II. The synthesis of a tetrapeptide. J Am Chem Soc 1963; 85: 2149-2153.
16 Akita E, Nakai S. Isolation and purification of inmunoglobulins from egg yolk. J Food Sci 1992; 57: 629-634. http://dx.doi.org/10.1111/j.1365-2621.1992.tb08058.x
17 Gassmann M, Thömmes P, Weiser T, Hübscher U. Efficient production of chicken egg yolk antibodies against a conserved mammalian protein. FASEB J 1990; 4: 2528-2532.
18 Jensenius J, Koch C. Antibodies packaged in eggs. Immunochemistry. 1997: IRL Press Oxford.
19 Hansen P, Scoble J, Hanson B, Hoogenraad N. Isolation and purification of immunoglobulins from chicken eggs using thiophilic interaction chromatography. J Inmunol Met 1998; 215: 1-7. http://dx.doi.org/10.1016/S0022-1759(98)00050-7
20 Hermanson G, Mallia A, Smith P. Immobilized Affinity Ligand Techniques. 1992; New York, USA: Academic Press Inc.
21 Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein - dye binding. Anal Biochem 1976; 72: 248 - 254. http://dx.doi.org/10.1016/0003-2697(76)90527-3
22 Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-685. http://dx.doi.org/10.1038/227680a0
23 Woof J, Burton D. Human antibody – Fc receptor interactions iluminated by cristal structures. Nat Rev Inmunol 2004; 4: 1- 11.
24 Perlmann H, Perlmann P. Enzyme-Linked Immunosorbent Assay. Cell Biology: A Laboratory Handbook. 1994: Academic Press Inc.
25 Wenthold R, Blahos J, Huh K, Petralia R. Detergent solubilization and immunoprecipitation of native NMDA receptors. In NMDA Receptor Protocols. 1999: Humana Press.
26 Akita E, Li-Chan E. Isolation of bovine immunoglobulin G subclasses from milk, colostrum and whey using immobilized egg yolk antibodies. J Dairy Sci 1998; 81: 54-63. http://dx.doi.org/10.3168/jds.S0022-0302(98)75550-X
27 Meulenaer B, Huyghebaert A. Isolation and purification of chicken egg yolk immunoglobulins: A review. Food Agricul Immunol 2001; 13: 275-288. http://dx.doi.org/10.1080/09540100120094537
28 Andersson O, Stenqvist A, Attersand A, Von G. Nucleotide sequence, genomic organization, and chromosomal localization of genes encoding the human NMDA receptor subunits NR3A and NR3B. Genomics 2001; 78: 178-184. http://dx.doi.org/10.1006/geno.2001.6666
29 Sasaki Y, Rothe T, Premkumar L, Das S, Cui J, Talantova M, et al. Characterization and comparison of the NR3A subunit of the NMDA receptor in recombinant systems and primary cortical neurons. J Neurophysiol 2002; 87: 2052-2063. http://dx.doi.org/10.1152/jn.00531.2001
30 Matsuda K, Kamiya Y, Matsuda S, Yuzaki M. Cloning and characterization of a novel NMDA receptor subunit NR3B: a dominant subunit that reduces calcium permeability. Mol Brain Res 2002; 10: 43- 52. http://dx.doi.org/10.1016/S0169-328X(02)00173-0
31 TMpred. Prediction of transmembrane regions and orientation Switzerland. http:/ /www.ch.embnet.org/software/ TMPRED_form.html.
32 Porath J, Maisano F, Belew M. Thiophilic adsorption – a new method for protein fractionation. FEBS Let 1985; 185: 306- 310. http://dx.doi.org/10.1016/0014-5793(85)80928-5
33 Villegas V, Zarante I, Lareo L. Estudio preliminar de los polimorfismos del gen GRIN-1 del receptor NMDA en una población sana colombiana. Univ Scient 2006; 11: 49-60.
34 Oyuela R, Lareo L, Mu-oz L, Morales L, Echevery S, Uribe A, et al. Efecto en el aprendizaje y la memoria espacial de un péptido sintético en ratas: estudio preliminar. Psicol Caribe 2004; 13: 1- 14.
35 Méndez G. Producción y purificación de IgY contra la subunidad NR3 del receptor de Glutamato tipo NMDA aislado de cerebro de rata.[Tesis de Maestria]. Bogotá, D.C, Colombia: Pontificia Universidad Javeriana, Facultad de Ciencias, Departamento de Nutrición y Bióquimica; 2005.
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dc.relation.citationedition.spa.fl_str_mv Núm. 1 , Año 2008 : Revista MVZ Córdoba Volumen 13(1) Enero-Abril 2008
dc.relation.citationissue.spa.fl_str_mv 1
dc.relation.citationvolume.spa.fl_str_mv 13
dc.relation.ispartofjournal.spa.fl_str_mv Revista MVZ Córdoba
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spelling Méndez, Ginac8c6aa86-06b2-436e-9054-22641f44ae9e-1Reyes, Edgarc2bd0373-ceb7-4b83-9bf4-ac1115a0b4ba-1Poutou, Raúl4593b291-45c3-421f-91e3-c9e3c1a4176b-1Quevedo, Balkysd8364c81-b0e7-4d0e-a9a9-265b0d60724f-1Lareo, Leonardofa16906a-bd66-4992-98e9-2c90fd3b4aaa-12008-01-01 00:00:002022-07-01T20:59:28Z2008-01-01 00:00:002022-07-01T20:59:28Z2008-01-010122-0268https://repositorio.unicordoba.edu.co/handle/ucordoba/562810.21897/rmvz.407https://doi.org/10.21897/rmvz.4071909-0544application/pdfspaUniversidad de Córdobahttps://creativecommons.org/licenses/by-nc-sa/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2https://revistamvz.unicordoba.edu.co/article/view/407NR3 subunitNMDA receptorIgYratbrain.Purificación de IgY contra la subunidad nr3 del receptor nmda de cerebro de rataPurificación de IgY contra la subunidad nr3 del receptor nmda de cerebro de rataArtículo de revistaJournal articleinfo:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1info:eu-repo/semantics/publishedVersionTexthttp://purl.org/redcol/resource_type/ARTREFhttp://purl.org/coar/version/c_970fb48d4fbd8a851 Dingledine R, Borges K, Bowie D, Traynelis S. The glutamate receptor ion channels. Pharmacol Rev 1999; 51: 7-61.2 Pérez I, Schulteis C, Contractor A, Lipton S, Trimmer J, Sucher N, et al. Assembly with the NR1 subunit is required for surface expression or NR3A-containing NMDA Receptors. J Neur 1999; 21: 1228- 1237.3 Cibarra S, Gahn L, Pecht G, Heinemann S, Sevarino K. Cloning and characterization of chi-1: A developmentally regulated member of a novel class of the ionotropic glutamate receptor family. J Neur 1995; 15: 6498-6508.4 Sucher N, Akbarian S, Chi C, Leclerc C, Awobuluyi M, Deitcher D, et al. Developmental and regional expression pattern of a novel NMDA receptor-like subunit (NMDAR-L) in the rodent brain. J Neur 1995; 15: 6509-6520.5 Das S, Sasaki Y, Rothe T, Premkumar L, Takasu M, Crandall J, et al. Increased NMDA current and spine density in mice lacking the NMDA receptor subunit NR3A. Nature 1998; 393: 377-381. http://dx.doi.org/10.1038/307486 Sun L, Margolis F, Shipley M, Lidow M. Identification of a long variant of mRNA encoding the NR3 subunit of the NMDA receptor: its regional distribution and developmental expression in the rat brain. FEBS Let 1998; 441: 392-396. http://dx.doi.org/10.1016/S0014-5793(98)01590-77 Nishi M, Heather H, Hai-Ping L, Mitsihiru K, Yasunori H. Motoneuron specific expression of NR3B, a novel NMDA type glutamate receptor subunit that works in a dominant negative manner. J Neur 2001; 21: 1-6.8 Madden D. The structure and function of glutamate receptor ion channels. Nature 2002; 3: 91-101.9 Morrison S, Mohammed M, Wims L, Trinh R, Etches R. Sequences in antibody molecules important for receptor mediated transport into the chicken egg yolk. Mol Immunol 2001; 38: 619-625. http://dx.doi.org/10.1016/S0161-5890(01)00095-510 Patterson R, Youngner J, Weigle W, Dixon F. Antibody production and transfer to egg yolk in chickens. J Inmunol 1962; 89: 272-278.11 Warr G, Magor K, Higgins D. IgY: clues to the origins if modern antibodies. Immunol Today 1995; 16: 392-398. http://dx.doi.org/10.1016/0167-5699(95)80008-512 Narat M. Production of antibodies in chickens. Food Technol Biotechnol 2003; 41: 259-267.13 IBCP. Pôle BioInformatique Lyonnais, Clustal W PBIL. URL disponible http:// npsa-pbil.ibcp.fr/cgi-bin/ npsa_automat.pl?page=/NPSA/ npsa_clustalw.html. 14 Caprino L, Han G. The 9- fluorenylmethoxycarbonyl group. J Org Chem 1972; 37: 3404-3409. http://dx.doi.org/10.1021/jo00795a00515 Merrifield R. Solid phase peptide synthesis II. The synthesis of a tetrapeptide. J Am Chem Soc 1963; 85: 2149-2153.16 Akita E, Nakai S. Isolation and purification of inmunoglobulins from egg yolk. J Food Sci 1992; 57: 629-634. http://dx.doi.org/10.1111/j.1365-2621.1992.tb08058.x17 Gassmann M, Thömmes P, Weiser T, Hübscher U. Efficient production of chicken egg yolk antibodies against a conserved mammalian protein. FASEB J 1990; 4: 2528-2532.18 Jensenius J, Koch C. Antibodies packaged in eggs. Immunochemistry. 1997: IRL Press Oxford.19 Hansen P, Scoble J, Hanson B, Hoogenraad N. Isolation and purification of immunoglobulins from chicken eggs using thiophilic interaction chromatography. J Inmunol Met 1998; 215: 1-7. http://dx.doi.org/10.1016/S0022-1759(98)00050-720 Hermanson G, Mallia A, Smith P. Immobilized Affinity Ligand Techniques. 1992; New York, USA: Academic Press Inc.21 Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein - dye binding. Anal Biochem 1976; 72: 248 - 254. http://dx.doi.org/10.1016/0003-2697(76)90527-322 Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-685. http://dx.doi.org/10.1038/227680a023 Woof J, Burton D. Human antibody – Fc receptor interactions iluminated by cristal structures. Nat Rev Inmunol 2004; 4: 1- 11.24 Perlmann H, Perlmann P. Enzyme-Linked Immunosorbent Assay. Cell Biology: A Laboratory Handbook. 1994: Academic Press Inc.25 Wenthold R, Blahos J, Huh K, Petralia R. Detergent solubilization and immunoprecipitation of native NMDA receptors. In NMDA Receptor Protocols. 1999: Humana Press.26 Akita E, Li-Chan E. Isolation of bovine immunoglobulin G subclasses from milk, colostrum and whey using immobilized egg yolk antibodies. J Dairy Sci 1998; 81: 54-63. http://dx.doi.org/10.3168/jds.S0022-0302(98)75550-X27 Meulenaer B, Huyghebaert A. Isolation and purification of chicken egg yolk immunoglobulins: A review. Food Agricul Immunol 2001; 13: 275-288. http://dx.doi.org/10.1080/0954010012009453728 Andersson O, Stenqvist A, Attersand A, Von G. Nucleotide sequence, genomic organization, and chromosomal localization of genes encoding the human NMDA receptor subunits NR3A and NR3B. Genomics 2001; 78: 178-184. http://dx.doi.org/10.1006/geno.2001.666629 Sasaki Y, Rothe T, Premkumar L, Das S, Cui J, Talantova M, et al. Characterization and comparison of the NR3A subunit of the NMDA receptor in recombinant systems and primary cortical neurons. J Neurophysiol 2002; 87: 2052-2063. http://dx.doi.org/10.1152/jn.00531.200130 Matsuda K, Kamiya Y, Matsuda S, Yuzaki M. Cloning and characterization of a novel NMDA receptor subunit NR3B: a dominant subunit that reduces calcium permeability. Mol Brain Res 2002; 10: 43- 52. http://dx.doi.org/10.1016/S0169-328X(02)00173-031 TMpred. Prediction of transmembrane regions and orientation Switzerland. http:/ /www.ch.embnet.org/software/ TMPRED_form.html.32 Porath J, Maisano F, Belew M. Thiophilic adsorption – a new method for protein fractionation. FEBS Let 1985; 185: 306- 310. http://dx.doi.org/10.1016/0014-5793(85)80928-533 Villegas V, Zarante I, Lareo L. Estudio preliminar de los polimorfismos del gen GRIN-1 del receptor NMDA en una población sana colombiana. Univ Scient 2006; 11: 49-60.34 Oyuela R, Lareo L, Mu-oz L, Morales L, Echevery S, Uribe A, et al. Efecto en el aprendizaje y la memoria espacial de un péptido sintético en ratas: estudio preliminar. Psicol Caribe 2004; 13: 1- 14.35 Méndez G. Producción y purificación de IgY contra la subunidad NR3 del receptor de Glutamato tipo NMDA aislado de cerebro de rata.[Tesis de Maestria]. Bogotá, D.C, Colombia: Pontificia Universidad Javeriana, Facultad de Ciencias, Departamento de Nutrición y Bióquimica; 2005.https://revistamvz.unicordoba.edu.co/article/download/407/475Núm. 1 , Año 2008 : Revista MVZ Córdoba Volumen 13(1) Enero-Abril 2008113Revista MVZ CórdobaPublicationOREORE.xmltext/xml2663http://172.16.14.198/bitstreams/655da8ed-30ba-4efb-ae42-0f3108b69d51/download7f1c6e57450696d66fcf0ff5f1febe0bMD51ucordoba/5628oai:172.16.14.198:ucordoba/56282023-10-06 00:45:11.233https://creativecommons.org/licenses/by-nc-sa/4.0/metadata.onlyhttp://172.16.14.198Repositorio Universidad de Córdobabdigital@metabiblioteca.com

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