Filpula D R, Lee S M, Link R P, Strausberg S L, Strausberg R L
Genex Corporation, Gaithersburg, Maryland 20877.
Biotechnol Prog. 1990 May-Jun;6(3):171-7. doi: 10.1021/bp00003a001.
The DOPA-rich polyphenolic protein secreted by the marine mussel Mytilus edulis establishes key chemical linkages in a water-resistant adhesive. Molecular cloning of the gene for this remarkable protein reveals its primary structure as one of the most repetitive proteins identified in the animal kingdom. Expression and purification of polyphenolic proteins from recombinant yeast have provided sufficient material to demonstrate adhesivity of these polypeptides in the laboratory. Adhesive tests reveal a water-resistant bonding capacity of the protein that is dependent on in vitro modification of tyrosine residues to DOPA and the subsequent oxidation to quinone.
贻贝分泌的富含多巴的多酚蛋白在一种防水粘合剂中建立关键化学连接。对这种非凡蛋白质的基因进行分子克隆，揭示了其一级结构是动物界中已鉴定出的最具重复性的蛋白质之一。从重组酵母中表达和纯化多酚蛋白，已提供了足够的材料在实验室中证明这些多肽的粘附性。粘附测试揭示了该蛋白质的防水结合能力，这种能力取决于酪氨酸残基在体外被修饰为多巴以及随后氧化为醌。
