کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2450952 1109666 2010 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Myosin filament depolymerizes in a low ionic strength solution containing l-histidine
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش تغذیه
پیش نمایش صفحه اول مقاله
Myosin filament depolymerizes in a low ionic strength solution containing l-histidine
چکیده انگلیسی

Myosin, one of the major myofibrillar proteins, forms a filamentous polymer and is insoluble in physiological and low ionic strength solutions. We have shown that myosin is soluble in a low ionic strength solution containing l-histidine. In this study, to clarify the role of l-histidine in the solubilization of myosin, we investigated effects of l-histidine on the filament formation and the morphology of myosin at a low ionic strength. In the presence of l-histidine, myosin formed a filamentous polymer in a physiological ionic strength solution and dispersed in a low ionic strength solution. Transmission electron microscopy showed that light meromyosin (LMM), the rod region of myosin, in a low ionic strength solution containing l-histidine was longer than that in a high ionic strength solution without l-histidine. l-histidine causes the elongation of LMM region of myosin contributing to the weakening of the myosin filament and the dissociation of myosin in a low ionic strength solution.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Meat Science - Volume 84, Issue 4, April 2010, Pages 742–746
نویسندگان
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