Glucose-6-phosphate Isomerase Is an Endogenous Inhibitor to Myofibril-Bound Serine Proteinase of Crucian Carp (Carassius auratus)
文献类型: 外文期刊
作者: Sun, Le-Chang 1 ; Zhou, Li-Gen 2 ; Du, Cui-Hong 1 ; Cai, Qiu-Feng 1 ; Hara, Kenji 3 ; Su, Wen-Jin 1 ; Cao, Min-Jie 1 ;
作者机构: 1.Jimei Univ, Coll Biol Engn, Key Lab Sci & Technol Aquaculture & Food Safety, Xiamen 361021, Peoples R China
2.Zhejiang Acad Agr Sci, Inst Food Proc, Hangzhou 310021, Zhejiang, Peoples R China
3.Nagasaki Univ, Fac Fisheries, Nagasaki 8528521, Japan
关键词: Crucian carp;glucose-6-phosphate isomerase;myofibril-bound serine proteinase;inhibitor;purification;immunoblotting
期刊名称:JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY ( 影响因子:5.279; 五年影响因子:5.269 )
ISSN:
年卷期:
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收录情况: SCI
摘要: Glucose-6-phosphate isomerase (GPI) was purified to homogeneity from the skeletal muscle of crucian carp (Carassius auratus) by ammonium sulfate fractionation, column chromatographies of Q-Sepharose, SP-Sepharose,"and Superdex 200 with a yield of 8.0%, and purification folds of 468. The molecular mass of GPI was 120 kDa as estimated by gel filtration, while on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), two subunits (55 and 65 kDa) were identified, suggesting that it is a heterodimer. Interestingly, GPI revealed specific inhibitory activity toward a myofibril-bound serine proteinase (MBSP) from crucian carp, while no inhibitory activity was identified toward other serine proteinases, such as white croaker MBSP and crucian carp trypsin. Kinetic analysis showed that GPI is a competitive inhibitor toward MBSP, and the K_i was 0.32 μM. Our present results indicated that the multifunctional protein GPI is an endogenous inhibitor to MBSP and may play a significant role in the regulation of muscular protein metabolism in vivo.
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