کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2021955 | 1069271 | 2006 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and initial characterization of a novel Porphyromonas gingivalis HmuY protein expressed in Escherichia coli and insect cells
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Purification and initial characterization of a novel Porphyromonas gingivalis HmuY protein expressed in Escherichia coli and insect cells Purification and initial characterization of a novel Porphyromonas gingivalis HmuY protein expressed in Escherichia coli and insect cells](/preview/png/2021955.png)
چکیده انگلیسی
Porphyromonas gingivalis acquires iron and heme from the host environment using gingipains, lipoproteins, and outer-membrane receptors. Recently, we identified and characterized a heme receptor HmuR. The hmuR gene is localized in an operon together with a hmuY gene encoding a putative heme-binding protein. The aim of this study was to overexpress and perform a preliminary analysis of the recombinant HmuY protein. We constructed and examined several recombinant HmuY variants which were overexpressed and purified from Escherichia coli and insect cells. Recombinant HmuY protein was expressed in insect cells at levels similar to those in E. coli cells. This protein is predominantly present in a monomeric form but also dimerizes and several other oligomerization forms were found. Hemin and ATP binding to the purified HmuY showed that this protein may play a regulatory function in hemin utilization in P. gingivalis.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 49, Issue 2, October 2006, Pages 299-306
Journal: Protein Expression and Purification - Volume 49, Issue 2, October 2006, Pages 299-306
نویسندگان
Teresa Olczak, Katarzyna Siudeja, Mariusz Olczak,