کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2022252 1069288 2006 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Purification and characterization of a functionally active Mycobacterium tuberculosis pyrroline-5-carboxylate reductase
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Purification and characterization of a functionally active Mycobacterium tuberculosis pyrroline-5-carboxylate reductase
چکیده انگلیسی

Pyrroline-5-carboxylate reductase (P5CR) plays an important role in the survival of Mycobacterium tuberculosis and is related to virulence of this pathogen. RT-PCR analysis indicated that proC, encoding P5CR, was expressed at the transcriptional level cultured in vitro. The His-rMtP5CR with an N-terminal His-tag (His-rMtP5CR) was firstly purified in Escherichia coli and rMtP5CR was obtained by removal of the N-terminal fusion partner using enterokinase. His-rMtP5CR had considerable β-pleated sheet analyzed by circular dichroism spectroscopy. The effect of pH, temperature, cations, denaturants, and detergents on the purified enzyme activity and stability was characterized. The N-terminal fusion partner was found to have very little effect on the biochemical properties of P5CR.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 45, Issue 1, January 2006, Pages 241–248
نویسندگان
, , , , , , ,