کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
11011741 | 1802855 | 2019 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Effect of nitric oxide on myofibrillar proteins and the susceptibility to calpain-1 proteolysis
ترجمه فارسی عنوان
اثر اکسید نیتریک در پروتئین های میوفیبریلر و حساسیت به پروتئولوز کلاپین-1
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
چکیده انگلیسی
This study was designed to investigate the nature of modification of myofibrillar proteins by nitric oxide (NO) and the extent to which S-nitrosylation alters their susceptibility to calpain-1 proteolysis. Isolated myofibrils from porcine semimembranosus muscle were incubated with the NO donor S-nitrosoglutathione (GSNO) at 0, 20, 50, 250, 1000â¯ÂµM for 30â¯min at 37â¯Â°C and then incubated with purified calpain-1. GSNO treatment decreased the thiol content of myofibrillar proteins and increased their intensity and amount of S-nitrosylation. GSNO caused the formation of proteins cross-linkage through intermolecular disulfide. More desmin and titin (T2, the degraded fragment of original titin) were degraded by calpain-1 when myofibrils were incubated with 1000â¯ÂµM GSNO. Incubation with 250 and 1000â¯ÂµM GSNO suppressed calpain-1-catalyzed cleavage of troponin-T. The data suggest that NO could change the redox state of myofibrillar proteins and subsequently affect the extent of proteolysis by calpain-1 in a protein-dependent manner.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 276, 15 March 2019, Pages 63-70
Journal: Food Chemistry - Volume 276, 15 March 2019, Pages 63-70
نویسندگان
Rui Liu, Steven Lonergan, Edward Steadham, Guanghong Zhou, Wangang Zhang, Elisabeth Huff-Lonergan,