کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5372288 | 1503983 | 2007 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Kinetic studies of protein L aggregation and disaggregation
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
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چکیده انگلیسی
We have investigated the aggregation of protein L in 25% (vol/vol) TFE and 10Â mM HCl. Under both conditions, aggregates adopt a fibrillar structure and bind dyes Congo Red and Thioflavin T consistent with the presence of amyloid fibrils. The kinetics of aggregation in 25% TFE suggest a linear-elongation mechanism with critical nucleus size of either two or three monomers. Aggregation kinetics in 10Â mM HCl show a prolonged lag phase prior to a rapid increase in aggregation. The lag phase is time-dependent, but the time dependence can be eliminated by the addition of pre-formed seeds. Disaggregation studies show that for aggregates formed in TFE, aggregate stability is a strong function of aggregate age. For example, after 200Â min of aggregation, 40% of the aggregation reaction is irreversible, while after 3Â days over 60% is irreversible. When the final concentration of the denaturant, TFE, is reduced from 5% to 0, the amount of reversible aggregation doubles. Disaggregation studies of aggregates formed in TFE and 10Â mM HCl reveal a complicated effect of pH on aggregate stability.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biophysical Chemistry - Volume 125, Issues 2â3, February 2007, Pages 350-359
Journal: Biophysical Chemistry - Volume 125, Issues 2â3, February 2007, Pages 350-359
نویسندگان
Troy Cellmer, Rutger Douma, Ansgar Huebner, John Prausnitz, Harvey Blanch,