Analysis of toxoplasma gondii proteins after Triton X-114 solubilization and hidropholic chromotograhy

Memórias do Instituto Oswaldo Cruz

Salvatore Giovanni De Simone¹  Helena C. B. Guedes¹  Izidro Bendet¹ 

[1] ,Instituto Oswaldo Cruz Departamento de Imunologia Rio de Janeiro,Brasil

关键词: Toxoplasma gondii;    Triton X-114;    hydrophobicities;    membrane proteins;    hydrophobic chromatography;    Toxoplasma gondii;    Triton X-114;    hidrofobicidade;    proteínas de membrana;    cromatografia hidrofóbica;   

DOI  :  10.1590/S0074-02761988000400019

来源: SciELO

【 摘 要 】

The distribution of the surface proteins of toxoplasma gondii radiodinated were studied using the phase separation technique and ability of binding in the phenyl-Sepharose column. Eight polypeptides with Mr 22 to 180 distributed exclusively in the detergent rich-phase, while six polypeptides with mol. wt. 15,000 to 76,000 distributed exclusively in the detergent poor-phase. Twopolypeptides with 15,000 and 70,000 distributed on both phase. All the polypeptides present in the detergent rich-phase binding in the phenyl-Sepharose column, and can be isolated in two peak according with their relative hydrophobicities.two polypeptides hydrophobic with Mr 60 and 66 recognized by human serum were isolated by the association of the two technique. Our result showed that the surface proteins of t. gondii present different degrees of hydrophobicity and that the use of hydrophobic interaction chromatography after Triton X-114 extraction may be an important isolation method of membrane proteins.

【 授权许可】

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