کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8294450 | 1536752 | 2018 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characterization of human ATP-binding cassette protein subfamily D reconstituted into proteoliposomes
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
In mammals, four ATP-binding cassette (ABC) proteins belonging to subfamily D have been identified. ABCD1â3 are located on peroxisomal membrane and play an important role in the transportation of various fatty acid-CoA derivatives, including very long chain fatty acid-CoA, into peroxisomes. ABCD4 is located on lysosomal membrane and is suggested to be involved in the transport of vitamin B12 from lysosomes to the cytosol. However, the precise transport mechanism by which these ABC transporters facilitate the import or export of substrate has yet to be well elucidated. In this study, the overexpression of human ABCD1â4 in the methylotrophic yeast Pichia pastoris and a purification procedure were developed. The detergent-solubilized proteins were reconstituted into liposomes. ABCD1â4 displayed stable ATPase activity, which was inhibited by AlF3. Furthermore, ABCD1â4 were found to possess an equal levels of acyl-CoA thioesterase activity. Proteoliposomes is expected to be an aid in the further biochemical characterization of ABCD transporters.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 496, Issue 4, 19 February 2018, Pages 1122-1127
Journal: Biochemical and Biophysical Research Communications - Volume 496, Issue 4, 19 February 2018, Pages 1122-1127
نویسندگان
Takumi Okamoto, Kosuke Kawaguchi, Shiro Watanabe, Rina Agustina, Toshiki Ikejima, Keisuke Ikeda, Minoru Nakano, Masashi Morita, Tsuneo Imanaka,