地中海贻贝贝壳肌棱柱层蛋白质组学分析  

Proteomic Analysis of Myostracum of Mytilus galloprovincialis Shell

作　　者：王新星[1] 高鹏[1] 鲍林飞 范美华[1] 廖智[1] 

机构地区：[1]浙江海洋学院海洋科学与技术学院,海洋生物资源及分子工程实验室,浙江舟山316022

出　　处：《浙江海洋学院学报（自然科学版）》2015年第5期444-451,共8页Journal of Zhejiang Ocean University(Natural Science Edition)

基　　金：浙江省自然科学基金项目(LY14C100001);蛋白质化学与发育生物学教育部重点实验室开放课题(2015DF02);国家大学生创新创业训练计划项目(01410340002)

摘　　要：贻贝贝壳与后闭壳肌形成紧密连接并由此介导了贝壳的闭合。为了解贻贝后闭壳肌-贝壳之间连接界面以及蛋白质分子组成,利用扫描电子显微镜、傅里叶红外光谱对地中海贻贝贝壳的微观结构、碳酸钙晶体构型进行分析;同时,采用酸抽提法获取地中海贻贝后闭壳肌痕部位肌棱柱层的贝壳基质蛋白,对酸可溶性蛋白和酸不溶性蛋白分别采用液质联用技术结合转录组数据库搜索,共鉴定61种贝壳基质蛋白。上述研究为深入了解贝壳的生物矿化机制以及肌肉-贝壳界面的无机相-有机相连接机理奠定了基础。The attachment of adductor muscle-shell in Mytilus mediates the closing of shells. For under- standing the mechanism and the molecular composition of this attachment, Scanning Electronic Microscopic and Fourier Transform Infrared Spectroscopy were used to explore the micro-structure and polymorph of mus- cle-shell attachment of Mytilus galloprovincialis. Furthermore, the protein composition of shell matrix from myostracum layer from adductor muscle scar of M. galloprovincialis was detected by a combination of LC-MS/ MS analysis with the Mytilus EST dataset search, which resulted in the identification of a total of 61 proteins from acid-soluble and acid-insoluble shell matrix proteins form myostracum of M. galloprovincialis shell. From this protein set, many novel shell proteins were identified which included proteins with possible link to biomin- eralization and certain uncharacterized proteins with unusual amino acid composition. This data would be use- ful in understanding the role of SMPs associated with the formation of myostracum. Further, the identified pro- tein set from the myostracum layer could provide a clue for exploring the mechanism of adductor muscle-shell attachment.

关 键 词：地中海贻贝 肌棱柱层 扫描电子显微镜 傅里叶红外光谱 蛋白质组学 

分 类 号：Q67[生物学—生物物理学]