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Molecular interconversion of cold-sensitive cytosolic 3,3',5-tri-iodo-L-thyronine-binding proteins from human erythrocytes: effect of cold, heat and pH treatments.
Fanjul, A N; Farías, R N.
Afiliación
  • Fanjul AN; Departamento de Bioquímica de la Nutrición, Instituto Superior de Investigaciones Biológicas (CONICET-UNT), San Miguel de Tucumman, Argentina.
Biochem J ; 290 ( Pt 2): 579-82, 1993 Mar 01.
Article en En | MEDLINE | ID: mdl-8452548
ABSTRACT
Cytosolic 3,3',5-tri-iodo-L-thyronine-binding proteins (CTBP I, II and IV species) from human red blood cells undergo rapid loss of activity at low temperatures. Cold treatment of CTBPs was accompanied by dissociation of the polymeric protein to the 60 kDa inactive monomer. Re-activation of the cold-inactivated CTBP IV by warming resulted in association of the monomer to the active polymeric form. A similar association-dissociation phenomenon was also obtained isothermically, though pH changes. We conclude that CTBP I and CTBP II are polymeric forms of CTBP IV.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Hormonas Tiroideas / Triyodotironina / Proteínas Portadoras / Eritrocitos / Proteínas de la Membrana Tipo de estudio: Diagnostic_studies Límite: Humans Idioma: En Revista: Biochem J Año: 1993 Tipo del documento: Article País de afiliación: Argentina

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Hormonas Tiroideas / Triyodotironina / Proteínas Portadoras / Eritrocitos / Proteínas de la Membrana Tipo de estudio: Diagnostic_studies Límite: Humans Idioma: En Revista: Biochem J Año: 1993 Tipo del documento: Article País de afiliación: Argentina