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Purification and characterisation of a phosphatidylcholine-binding protein from duck Biceps femoris muscle

文献类型： 外文期刊

作者： Wang, D. Y. 1 ; Zhang, M. H. 1 ; Liu, F. 1 ; Zhu, Y. Z. 1 ; Xu, W. M. 1 ;

作者机构： 1.Jiangsu Acad Agr Sci, Inst Agr Prod Proc, Nanjing 210014, Jiangsu, Peoples R China

关键词： characterisation;phospholipase A(2);purification

期刊名称：ANIMAL PRODUCTION SCIENCE （ 影响因子：1.533； 五年影响因子：1.779 ）

ISSN： 1836-0939

年卷期： 2014 年 54 卷 2 期

页码：

收录情况： SCI

摘要： The interaction between protein and phospholipids is a widespread phenomenon involving several physiological events in postmortem muscle. We hereby report a method for one-step purification of a phosphatidylcholine-binding (PC-binding) protein from duck Biceps femoris muscle with relatively high purity and yield using ion-exchange chromatography. This PC-binding protein has an inhibitory effect on the activity of phospholipase A(2) (PLA(2)). A decrease (similar to 62.3%) in PLA(2) activity was observed. It had a strong affinity to bind PC at pH range of 6.2-6.8 with a peak at pH 6.6 (13.36 +/- 0.48 g PC/g protein); in addition, raising ATP content from 1 to 5 mol/mL enhanced the binding capacity. The PC-binding protein plays a potential role in the integrity of membrane and meat quality.

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