RESUMO
An investigation of the binding of native and recombinant human serum albumin and bovine serum albumin on three thiophilic gels, PyS, 2S, and 3S was performed. In addition to these proteins, we studied serum albumins from several species such as goat, rabbit, guinea pig, rat, hamster, baboon, and pig. Our results reveal that recombinant human serum albumin (rHSA) binds completely to PyS whereas native human serum albumin and bovine serum albumin bind only partially to PyS. The binding affinities of rHSA, human serum albumin and bovine serum albumin to 2S and 3S gels are less than their binding to PyS. Serum albumins from goat, rabbit, guinea pig, rat, hamster, baboon, and pig bind much stronger to 3S gel than human and bovine serum albumins. The binding of pig and hamster serum albumins is stronger than that of rat, goat, baboon, and rabbit.
Assuntos
Cromatografia Líquida de Alta Pressão/métodos , Albumina Sérica/química , Animais , Bovinos , Humanos , Proteínas Recombinantes/química , Espectrometria de Fluorescência , Espectrofotometria UltravioletaRESUMO
Transferrins are a class of iron-binding proteins widely distributed in biological fluids. All transferrins possess two metal binding sites, each of which can bind a ferric iron. Transferrins play a major role in plasma iron transport and have anti-bacterial, anti-inflammatory, and immunological functions. Lactoferrin is an iron-binding bilobal protein of the transferrin family found in neutrophilic leukocytes and external secretion of mammals. In an earlier communication, we have shown that both human serum transferrin and lactoferrin bind to 3S-gel. Ovotransferrin, the major egg-white protein, is an avian transferrin. In this paper, the details of the binding of mammalian and avian transferrins to 2S gel is presented. Both, apo and holo ovotransferrin, bind to 2S T-gel. Holo and apo lactoferrin from other mammalian species such as cow, rabbit, dog, mouse, and rat bind to T-gel.
Assuntos
Cromatografia Líquida de Alta Pressão/métodos , Transferrina/química , Animais , Aves , Mamíferos , Especificidade da Espécie , Transferrina/metabolismoRESUMO
Lactoferrin and serum transferrin, the iron-binding proteins, are widely distributed in biological fluids. Transferrins have many biological functions: anti-bacterial, anti-inflammatory, and immunoregulatory. A facile monitoring of the concentration of transferrins in biological fluids may have medical relevance. Thiophilic-interaction chromatography of transferrins may provide an efficient means for their quantitation in serum.
