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Registro Completo |
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Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
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Data corrente: |
21/05/2024 |
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Data da última atualização: |
21/05/2024 |
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Autoria: |
GOLDFARB, M. |
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Título: |
Two-dimensional electrophoresis and computer imaging: quantitation of human milk casein. |
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Ano de publicação: |
1999 |
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Fonte/Imprenta: |
Electrophoresis, v. 20, n. 4/5, p. 870-874, Apr-May, 1999. |
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DOI: |
10.1002/(SICI)1522-2683(19990101)20:4/5<870::AID-ELPS870>3.0.CO;2-E. |
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Idioma: |
Inglês |
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Conteúdo: |
Abstract: Because human casein does not precipitate from milk at its isoelectric point as does bovine casein, there is no easy method of quantitation. Casein represents only approximately 30% of the protein fraction in human milk, and the complex methods necessary for isolation cannot be used easily with small samples in a survey of a large number of mothers. Two-dimensional electrophoresis coupled with computer imaging has the potential to compare and quantitate proteins expeditiously using a small sample size. Iso-Dalt, a denaturing methodology, separates the casein micelle into its component parts, beta-casein, kappa-casein, parakappa-casein and casomorphins. Identification of these spots was made by immunoassay of a Western blot with monoclonal anti-human casein. Two spots at 24 kDa and 26 kDa, thought to be phosphorylated isomers of beta casein, were selected for quantitation. Milk samples from 20 mothers, 8 weeks post partum, were run on two-dimensional (2-D) gels; a slide was taken of each silver-stained gel with a Kodak control strip; the slide was scanned into powerMac Photoshop 3 with a Polaroid-Sprintscan; spots were isolated using “threshold”, “mask” with IPTK (Imaging Processing Tool Kit, Reindeer Games) a Photoshop plug-in, and transferred to the NIH-Image program. Using an NIH-Image gel macro (Thomas Seebacher), the area and integrated density of the spots were measured. The Kodak control scale provided calibration and conversion to OD units. Visual scanning of the gels and computer units indicated a wide range of concentrations. To understand the range in units of weight, a standard was generated using bovine alpha casein (Sigma). Measurements will be used in a statistical program, Statview (Abacus), in an attempt to correlate information from a questionaire with casein concentration. MenosAbstract: Because human casein does not precipitate from milk at its isoelectric point as does bovine casein, there is no easy method of quantitation. Casein represents only approximately 30% of the protein fraction in human milk, and the complex methods necessary for isolation cannot be used easily with small samples in a survey of a large number of mothers. Two-dimensional electrophoresis coupled with computer imaging has the potential to compare and quantitate proteins expeditiously using a small sample size. Iso-Dalt, a denaturing methodology, separates the casein micelle into its component parts, beta-casein, kappa-casein, parakappa-casein and casomorphins. Identification of these spots was made by immunoassay of a Western blot with monoclonal anti-human casein. Two spots at 24 kDa and 26 kDa, thought to be phosphorylated isomers of beta casein, were selected for quantitation. Milk samples from 20 mothers, 8 weeks post partum, were run on two-dimensional (2-D) gels; a slide was taken of each silver-stained gel with a Kodak control strip; the slide was scanned into powerMac Photoshop 3 with a Polaroid-Sprintscan; spots were isolated using “threshold”, “mask” with IPTK (Imaging Processing Tool Kit, Reindeer Games) a Photoshop plug-in, and transferred to the NIH-Image program. Using an NIH-Image gel macro (Thomas Seebacher), the area and integrated density of the spots were measured. The Kodak control scale provided calibration and conversion to OD units. Visual scanning o... Mostrar Tudo |
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Palavras-Chave: |
Computer imaging. |
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Thesaurus Nal: |
Casein; Humans; Milk; Two-dimensional gel electrophoresis; Western blotting. |
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Categoria do assunto: |
-- |
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Marc: |
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001 2164387
005 2024-05-21
008 1999 bl uuuu u00u1 u #d
024 7 $a10.1002/(SICI)1522-2683(19990101)20:4/5<870::AID-ELPS870>3.0.CO;2-E.$2DOI
100 1 $aGOLDFARB, M.
245 $aTwo-dimensional electrophoresis and computer imaging$bquantitation of human milk casein.$h[electronic resource]
260 $c1999
520 $aAbstract: Because human casein does not precipitate from milk at its isoelectric point as does bovine casein, there is no easy method of quantitation. Casein represents only approximately 30% of the protein fraction in human milk, and the complex methods necessary for isolation cannot be used easily with small samples in a survey of a large number of mothers. Two-dimensional electrophoresis coupled with computer imaging has the potential to compare and quantitate proteins expeditiously using a small sample size. Iso-Dalt, a denaturing methodology, separates the casein micelle into its component parts, beta-casein, kappa-casein, parakappa-casein and casomorphins. Identification of these spots was made by immunoassay of a Western blot with monoclonal anti-human casein. Two spots at 24 kDa and 26 kDa, thought to be phosphorylated isomers of beta casein, were selected for quantitation. Milk samples from 20 mothers, 8 weeks post partum, were run on two-dimensional (2-D) gels; a slide was taken of each silver-stained gel with a Kodak control strip; the slide was scanned into powerMac Photoshop 3 with a Polaroid-Sprintscan; spots were isolated using “threshold”, “mask” with IPTK (Imaging Processing Tool Kit, Reindeer Games) a Photoshop plug-in, and transferred to the NIH-Image program. Using an NIH-Image gel macro (Thomas Seebacher), the area and integrated density of the spots were measured. The Kodak control scale provided calibration and conversion to OD units. Visual scanning of the gels and computer units indicated a wide range of concentrations. To understand the range in units of weight, a standard was generated using bovine alpha casein (Sigma). Measurements will be used in a statistical program, Statview (Abacus), in an attempt to correlate information from a questionaire with casein concentration.
650 $aCasein
650 $aHumans
650 $aMilk
650 $aTwo-dimensional gel electrophoresis
650 $aWestern blotting
653 $aComputer imaging
773 $tElectrophoresis$gv. 20, n. 4/5, p. 870-874, Apr-May, 1999.
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| 2. |  | HAYASHIDA, R.; QUEIROZ, A. P. de; BUENO, A. de F. Interação entre modos de liberação de Telenomus podisi: plantio direto (SPD) e convencional (SC). In: SIMPÓSIO DE CONTROLE BIOLÓGICO, 16., 2019, Londrina. Controle biológico: da academia ao campo, rumo à sustentabilidade: anais. Londrina: Sociedade Entomológica do Brasil: Embrapa Soja: Universidade Estadual de Londrina, 2019. 495 p. Organizadores: Adeney de Freitas Bueno, Pedro Manuel Oliveira Janeiro, Michele Potrich, Geraldo Andrade Carvalho. p. 325.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Soja. |
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| 6. | | LUSKI, P. G. G.; QUEIROZ, A. P.; BUENO, A. de F.; NEVES, P. M. O. J. Eficiência de Spodoptera frugiperda multiple nucleopolyhedrovirus (SfMNPV) associado com herbicidas no milho e soja em campo. In: CONGRESSO BRASILEIRO DE ENTOMOLOGIA, 27.; CONGRESSO LATINO-AMERICANO DE ENTOMOLOGIA, 10., 2018, Gramado, RS. Saúde, ambiente e agricultura: anais. Santo Antonio de Goiás: SEB: UFSM, 2018. v. 2. resumo. p. 1620.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Soja. |
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| 7. | | QUEIROZ, A. P.; TAGUTI, E. A.; BUENO, A. F.; GRANDE, M. L. M.; COSTA, C. O. Host preferences of Telenomus podisi (Hymenoptera: Scelionidae): parasitism on eggs of Dichelops melacanthus,Euschistus heros, and Podisus nigrispinus (Hemiptera: Pentatomidae). Neotropical entomology, v. 47, p. 543-552, 2018.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 2 |
| Biblioteca(s): Embrapa Soja. |
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| 9. | | POMARI, A. F.; BUENO, A. de F.; QUEIROZ, A. P.; BORTOLI, S. A. de. Biologia de Telenomus remus em ovos de Spodoptera frugiperda de parasitoides provenientes de criação massal em ovos de Corcyra cephalonica por diferentes gerações. In: SIMPÓSIO DE CONTROLE BIOLÓGICO, 13., 2013, Bonito, MS. Anais... Brasília, DF: Embrapa, 2013. 1 CD-ROM. SICONBIOL.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Soja. |
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| 12. | | LUSKI, P. G. G.; QUEIROZ, A. P.; BUENO, A. de F.; NEVES, P. M. O. J. Compatibilidade do Baculovirus spodoptera (SfMNPV) em mistura com herbicidas no milho em laboratório. In: CONGRESSO BRASILEIRO DE ENTOMOLOGIA, 27.; CONGRESSO LATINO-AMERICANO DE ENTOMOLOGIA, 10., 2018, Gramado, RS. Saúde, ambiente e agricultura: anais. Santo Antonio de Goiás: SEB: UFSM, 2018. v. 2. resumo. p. 1617.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Soja. |
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| 13. | | BORTOLOTTO, O. C.; BUENO, A. F.; STOPA, Y. K.; SILVA, G. V.; QUEIROZ, A. P. Development of Dichelops melacanthus and its egg parasitoid Telenomus podisi reared on Bt-soybean MON 87701 x MON 89788 and its near conventional isoline under different temperatures. Anais da Academia Brasileira de Ciências, Rio de Janeiro, v. 88, n. 2, p. 1023-1034, 2016.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
| Biblioteca(s): Embrapa Soja. |
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| 14. | | GRANDE, M. L. M.; QUEIROZ, A. P.; BUENO, A. de F.; GONÇALVES, J.; BRAZ, E. C. Efeito da cápsula de liberação na proteção de pupas de Trichogramma pretiosum, Telenomus remus e Telenomus podisi em campo. In: SIMPÓSIO DE CONTROLE BIOLÓGICO, 16., 2019, Londrina. Controle biológico: da academia ao campo, rumo à sustentabilidade: anais. Londrina: Sociedade Entomológica do Brasil: Embrapa Soja: Universidade Estadual de Londrina, 2019. 495 p. Organizadores: Adeney de Freitas Bueno, Pedro Manuel Oliveira Janeiro, Michele Potrich, Geraldo Andrade Carvalho. p. 184.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Soja. |
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| 19. | | QUEIROZ, A. P.; POMARI, A. F.; BUENO, A. de F.; BORTOLI, S. A. de. Influência da umidade relativa nas características biológicas deTelenomus remus em ovos Spodoptera frugiperda e Corcyra cephalonica. In: SIMPÓSIO DE CONTROLE BIOLÓGICO, 13., 2013, Bonito, MS. Anais... Brasília, DF: Embrapa, 2013. 1 CD-ROM. SICONBIOL.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Soja. |
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| Registros recuperados : 104 | |
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