کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10769263 | 1050820 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Kinetics of calmodulin binding to calcineurin
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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
Calcineurin (CaN) binds Ca2+-saturated calmodulin (CaM) with relatively high affinity; however, an accurate steady-state Kd value has not been determined. In this report, we describe, using steady-state and stopped-flow fluorescence techniques, the rates of association and dissociation of Ca2+-saturated CaM from CaN heterodimer (CaNA/CaNB) and CaNA only. The rate of Ca2+/CaM association was determined to be 4.6Â ÃÂ 107Â Mâ1Â sâ1. The rate of Ca2+/CaM dissociation from CaN was slower than previously reported and was approximately 0.0012Â sâ1. In preparations of CaNA alone (no regulatory CaNB subunit), the dissociation rate was slowed further to 0.00026Â sâ1. From these data we calculate a Kd for binding of Ca2+-saturated CaM to CaN of 28Â pM. This Kd is significantly lower than previously reported estimates of â¼1Â nM and indicates that CaN is one of the highest affinity CaM-binding proteins identified to date.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 334, Issue 2, 26 August 2005, Pages 674-680
Journal: Biochemical and Biophysical Research Communications - Volume 334, Issue 2, 26 August 2005, Pages 674-680
نویسندگان
Andrea R. Quintana, Dan Wang, Joanna E. Forbes, M. Neal Waxham,