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Multiple protein stationary phases: a review.
Singh, N S; Habicht, K-L; Dossou, K S S; Shimmo, R; Wainer, I W; Moaddel, R.
Afiliación
  • Singh NS; Biomedical Research Center, National Institute on Aging, National Institutes of Health, 251 Bayview Boulevard, Suite 100, Baltimore, MD 21224, USA.
  • Habicht KL; Department of Natural Sciences, Institute of Mathematics and Natural Sciences, Tallinn University, Narva mnt. 29, 10120 Tallinn, Estonia.
  • Dossou KS; Biomedical Research Center, National Institute on Aging, National Institutes of Health, 251 Bayview Boulevard, Suite 100, Baltimore, MD 21224, USA.
  • Shimmo R; Department of Natural Sciences, Institute of Mathematics and Natural Sciences, Tallinn University, Narva mnt. 29, 10120 Tallinn, Estonia.
  • Wainer IW; Biomedical Research Center, National Institute on Aging, National Institutes of Health, 251 Bayview Boulevard, Suite 100, Baltimore, MD 21224, USA.
  • Moaddel R; Biomedical Research Center, National Institute on Aging, National Institutes of Health, 251 Bayview Boulevard, Suite 100, Baltimore, MD 21224, USA. Electronic address: moaddelru@grc.nia.nih.gov.
J Chromatogr B Analyt Technol Biomed Life Sci ; 968: 64-8, 2014 Oct 01.
Article en En | MEDLINE | ID: mdl-24780640
Cellular membrane affinity chromatography stationary phases have been extensively used to characterize immobilized proteins and provide a direct measurement of multiple binding sites, including orthosteric and allosteric sites. This review will address the utilization of immobilized cellular and tissue fragments to characterize multiple transmembrane proteins co-immobilized onto a stationary phase. This approach will be illustrated by demonstrating that multiple transmembrane proteins were immobilized from cell lines and tissue fragments. In addition, the immobilization of individual compartments/organelles within a cell will be discussed and the changes in the proteins binding/kinetics based on their location.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Inmovilizadas / Proteínas de la Membrana Límite: Humans Idioma: En Revista: J Chromatogr B Analyt Technol Biomed Life Sci Asunto de la revista: ENGENHARIA BIOMEDICA Año: 2014 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Inmovilizadas / Proteínas de la Membrana Límite: Humans Idioma: En Revista: J Chromatogr B Analyt Technol Biomed Life Sci Asunto de la revista: ENGENHARIA BIOMEDICA Año: 2014 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos