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
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Kinetics of calmodulin binding to calcineurin
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 4.6 × 107 M−1 s−1. The rate of Ca2+/CaM dissociation from CaN was slower than previously reported and was approximately 0.0012 s−1. In preparations of CaNA alone (no regulatory CaNB subunit), the dissociation rate was slowed further to 0.00026 s−1. From these data we calculate a Kd for binding of Ca2+-saturated CaM to CaN of 28 pM. This Kd is significantly lower than previously reported estimates of ∼1 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
نویسندگان
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