Protein gradients in byssal threads of some marine bivalve molluscs.
Protein gradients in byssal threads of some marine bivalve molluscs.
复制标题
一些海洋双壳类软体动物足丝中的蛋白质梯度。
DOI：
10.1002/jez.1402400102
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
Waite,JH
中科院分区：
文献类型：
--
作者：
Mascolo,JM;Waite,JH
许多海洋双壳类软体动物产生深海丝以附着在固体基质上。紫贻贝Mytilus edulis、M. californianus、Geukensia demissa、Atrina vexillum和A.通过氨基酸分析来分析刚性，以确定化学组成是否作为螺纹段中位置的函数保持恒定。非线性纵向蛋白梯度，可能涉及胶原蛋白和弹性蛋白，被发现在Mytilus物种。在这些中，胶原蛋白在线的远端三分之一处达到峰值。在Geukensia和Atrinaspecies，虽然这两个在组成上有很大的不同，有一个明确的不变组成的线程内的每个物种作为一个功能的位置在线程。所有被检查品种的线尖端处的粘合剂斑块在成分上与线的其余部分有很大不同。一些双壳类的螺纹中的蛋白质梯度可能反映了在高能环境中为应对暴露的栖息地而进化的特定适应。
Many marine bivalve molluscs produce byssal threads for attachment to solid substrata. Small (< 10 mm) consecutive sections of the byssal threads ofMytilus edulis, M. californianus, Geukensia demissa, Atrina vexillum, andA. rigidawere analyzed by amino acid analysis to determine if chemical composition remains constant as a function of location in thread segments. Nonlinear longitudinal protein gradients, probably involving collagen and an elastic protein, were found in theMytilusspecies. In these, collagen peaks in the distal third of the thread. InGeukensiaand theAtrinaspecies, although the two differed greatly in composition, there is a clear nonvariability in composition of the thread within each species as a function of location in the thread. The adhesive plaque at the tip of the thread of all species examined differs substantially in composition from the remainder of the thread. Protein gradients in the threads of some bivalves may reflect specific adaptations evolved to respond to exposed habitats in high‐energy environments.