کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2050971 1074187 2007 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Calpastatin simultaneously binds four calpains with different kinetic constants
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Calpastatin simultaneously binds four calpains with different kinetic constants
چکیده انگلیسی

Calpastatin is the endogenous, specific protein inhibitor of the calcium-dependent protease, calpain. Using an active site knock-out m-calpain mutant we have studied the enzyme’s calcium-dependent binding to calpastatin by surface plasmon resonance without the complication of proteolysis. Calpastatin was capable of simultaneously binding four molecules of calpain. Its four inhibitory domains (CAST1, 2, 3, and 4) were individually expressed in Escherichia coli and the kinetics of their interaction with calpain was separately compared. Their Kd values ranged from picomolar to nanomolar in the order CAST1 > 4 > 3 > 2. They have similar kon values but the koff values ranged over three orders of magnitude and can account for the differences in affinity.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 581, Issue 16, 26 June 2007, Pages 2894–2898
نویسندگان
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