STRUCTURAL AND FUNCTIONAL REPETITION IN A MARINE MUSSEL ADHESIVE PROTEIN

被引:116
作者
FILPULA, DR [1 ]
LEE, SM [1 ]
LINK, RP [1 ]
STRAUSBERG, SL [1 ]
STRAUSBERG, RL [1 ]
机构
[1] GENEX CORP,16020 IND DR,GAITHERSBURG,MD 20877
关键词
D O I
10.1021/bp00003a001
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
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. Copyright © 1990 American Institute of Chemical Engineers (AIChE)
引用
收藏
页码:171 / 177
页数:7
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