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Transferrin as a model system for method development to study structure, dynamics and interactions of metalloproteins using mass spectrometry.
Kaltashov, Igor A; Bobst, Cedric E; Zhang, Mingxuan; Leverence, Rachael; Gumerov, Dmitry R.
Afiliación
  • Kaltashov IA; Department of Chemistry, University of Massachusetts-Amherst, Amherst, MA, USA. Kaltashov@chem.umass.edu
Biochim Biophys Acta ; 1820(3): 417-26, 2012 Mar.
Article en En | MEDLINE | ID: mdl-21726602
ABSTRACT

BACKGROUND:

Transferrin (Tf) is a paradigmatic metalloprotein, which has been extensively studied in the past and still is a focal point of numerous investigation efforts owing to its unique role in iron homeostasis and enormous promise as a component of a wide range of therapies. SCOPE OF REVIEW Electrospray ionization mass spectrometry (ESI MS) is a potent analytical tool that has been used successfully to study various properties of Tf and Tf-based products, ranging from covalent structure and metal binding to conformation and interaction with their physiological partners. MAJOR

CONCLUSIONS:

Various ESI MS-based techniques produce unique information on Tf properties and behavior that is highly complementary to information provided by other experimental techniques. GENERAL

SIGNIFICANCE:

The experimental ESI MS-based techniques developed for Tf studies are not only useful for understanding of fundamental aspects of the iron-binding properties of this protein and optimizing Tf-based therapeutic products, but can also be applied to study a range of other metalloproteins. This article is part of a Special Issue entitled Transferrins Molecular mechanisms of iron transport and disorders.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Transferrina / Hierro Límite: Humans Idioma: En Revista: Biochim Biophys Acta Año: 2012 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Transferrina / Hierro Límite: Humans Idioma: En Revista: Biochim Biophys Acta Año: 2012 Tipo del documento: Article País de afiliación: Estados Unidos