LOCATION AND ANALYSIS OF BYSSAL STRUCTURAL PROTEINS OF MYTILUS-EDULIS
LOCATION AND ANALYSIS OF BYSSAL STRUCTURAL PROTEINS OF MYTILUS-EDULIS
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DOI：
10.1002/jmor.1051890207
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发表时间：
1986-08-01
影响因子：
1.5
通讯作者：
WAITE, JH
中科院分区：
文献类型：
--
作者：
BENEDICT, CV;WAITE, JH
海洋贻贝的无细胞附着器官（足丝）由从贻贝身体发出的丝线组成，并附着在粘合盘上，这些粘合盘将丝线固定在岩石、沙子和其他贝类上。三种蛋白质已通过免疫组织学方法纯化并定位到足丝的特定起源。在乳丝区域的基质中发现了亚基分子量为53,000、55,000和65,000的胶原蛋白。它的 73,000 MW 前体是从动物身体附近区域的足腺中提取的，并通过免疫交叉反应进行鉴定。在足丝的所有区域都发现了一种富含胱氨酸的酸性蛋白质，与第三种蛋白质（多酚蛋白质）相关。含有左旋多巴的多酚蛋白出现在整个线和粘附斑块的皮质中以及基底-斑块界面处。这种蛋白质的抗血清会对足部酚腺中的球形囊泡进行染色。使用免疫电泳方法，多酚蛋白和富含胱氨酸的蛋白被证明随着足丝的老化形成高分子量聚集体。
The acellular attachment organ (byssus) of the marine mussel Mytilus edulis L. is composed of threads that emanate from the body of the mussel to adhesive discs that anchor the threads to rocks, sand and other mussels. Three proteins have been purified by immunohistologic methods and located to specific origins of the byssus. A collagenous protein with subunit molecular weights of 53,000, 55,000 and 65,000 is found in the matrix of the lactic thread region. Its 73,000-MW precursor was extracted from foot glands in the area proximal to the animal body and was identified by immune cross-reactivity. A cystine-rich, acidic protein was found in all regions of the byssus associated with a third protein, the polyphenolic protein. The L-dopa-containing polyphenolic protein appears in the cortex of the entire thread and adhesive plaque and at the substrate-plaque interface. Antiserum to this protein stains spherical vesicles in the phenol gland of the foot. Using immuno-electrophoretic methods, the polyphenolic protein and the cystine-rich protein were shown to form high molecular weight aggregates with aging of the byssus.