کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5510420 | 1539121 | 2017 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Molecular cloning and characterization of glycogen synthase in Eriocheir sinensis
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کلمات کلیدی
Moulting cycleIMACGlucosyltransferase activityEriocheir sinensisGBEUDPPP1G6PGSK-3GCsuridine diphosphate - uridine دی فسفاتGlycogen branching enzyme - آنزیم شاخه ای گلیکوژنSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدsodium dodecylsulfate polyacrylamide gel electrophoresis - الکتروفورز ژل پلی اکریللید سدیم دودسیل سولفاتRace - مسابقهprotein phosphatase-1 - پروتئین فسفاتاز-1immobilized metal affinity chromatography - کروماتوگرافی وابسته به فلز متمرکزglucose-6-phosphate - گلوکز 6-فسفاتGlycogenin - گلیکوزینglycogen synthase kinase-3 - گلیکوزین سنتاز کیناز 3Glycogen - گلیکوژنglycogen synthase - گلیکوژن سنتاز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Glycogen plays an important role in glucose and energy homeostasis at cellular and organismal levels. In glycogen synthesis, glycogen synthase (GS) is a rate-limiting enzyme catalysing the addition of α-1,4-linked glucose units from (UDP)3-glucose to a nascent glycogen chain using glycogenin (GN) as a primer. While studies on mammalian liver GS (GYS2) are numerous, enzymes from crustaceans, which also use glycogen and glucose as their main energy source, have received less attention. In the present study, we amplified full-length GS cDNA from Eriocheir sinensis. Tissue expression profiling revealed the highest expression of GS in the hepatopancreas. During moulting, GS expression and activity declined, and glycogen levels in the hepatopancreas were reduced. Recombinant GS was expressed in Escherichia coli Rosetta (DE3), and induction at 37 °C or 16 °C yielded EsGS in insoluble inclusion bodies (EsGS-I) or in soluble form (EsGS-S), respectively. Enzyme activity was measured in a cell-free system containing glucose-6-phosphate (G6P), and both forms possessed glycosyltransferase activity, but refolded EsGS-I was more active. Enzyme activity of both GS and EsGS-I in the hepatopancreas was optimum at 25 °C, which is coincident with the optimum growth temperature of Chinese mitten crab, and higher (37 °C) or lower (16 °C) temperatures resulted in lower enzyme activity. Taken together, the results suggest that GS may be important for maintaining normal physiological functions such as growth and reproduction.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology - Volume 214, December 2017, Pages 47-56
Journal: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology - Volume 214, December 2017, Pages 47-56
نویسندگان
Ran Li, Li-Na Zhu, Li-Qi Ren, Jie-Yang Weng, Jin-Sheng Sun,