کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1938916 1050750 2006 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Functional characterisation of ganglioside-induced differentiation-associated protein 1 as a glutathione transferase
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Functional characterisation of ganglioside-induced differentiation-associated protein 1 as a glutathione transferase
چکیده انگلیسی

Mutations in the ganglioside-induced differentiation-associated protein 1 (GDAP1) gene have been linked with Charcot–Marie-Tooth (CMT) disease. This protein, and its paralogue GDAP1L1, appear to be structurally related to the cytosolic glutathione S-transferases (GST) including an N-terminal thioredoxin fold domain with conserved active site residues. The specific function, of GDAP1 remains unknown. To further characterise their structure and function we purified recombinant human GDAP1 and GDAP1L1 proteins using bacterial expression and immobilised metal affinity chromatography. Like other cytosolic GSTs, GDAP1 protein has a dimeric structure. Although the full-length proteins were largely insoluble, the deletion of a proposed C-terminal transmembrane domain allowed the preparation of soluble protein. The purified proteins were assayed for glutathione-dependent activity against a library of ‘prototypic’ GST substrates. No evidence of glutathione-dependent activity or an ability to bind glutathione immobilised on agarose was found.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 347, Issue 4, 8 September 2006, Pages 859–866
نویسندگان
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