کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1937634 | 1050721 | 2007 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Assay optimization and kinetic profile of the human and the rabbit isoforms of 11β-HSD1
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Assay conditions for the 11β-hydroxysteroid dehydrogenase have been optimized by adding phospholipids in the media buffer to increase and stabilize the enzymatic activity. The presence of phospholipids greatly facilitates the study of the binding of cortisone and NADPH at the enzyme catalytic site. Kinetic analyses conducted with the human and rabbit enzyme isoforms suggest that both enzymes behave according to an ordered sequential bi-bi mechanism where the NADPH is the first to bind at the active site followed by cortisone. The equilibrium dissociation constant, Kia as well as the apparent Michaelis-Menten constants Kma, Kmb, kcata, and kcatb for NADPH and cortisone, have been determined to be 147.5 μM, 14.4 μM, 43.8 nM, 0.21 minâ1, and 0.27 minâ1, respectively, for the human enzyme and 41.1 μM, 3.1 μM, 161.7 nM, 0.49 minâ1, and 0.52 minâ1, respectively, for the rabbit enzyme.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 357, Issue 2, 1 June 2007, Pages 561-566
Journal: Biochemical and Biophysical Research Communications - Volume 357, Issue 2, 1 June 2007, Pages 561-566
نویسندگان
Arturo Castro, Jeff X. Zhu, Gordon R. Alton, Paul Rejto, Jacques Ermolieff,