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Tetranectin, a trimeric plasminogen-binding C-type lectin.

T L Holtet·J H Graversen·I Clemmensen·H C Thøgersen·M Etzerodt
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Abstract

Tetranectin, a plasminogen-binding protein belonging to the family of C-type lectins, was expressed in E. coli and converted to its native form by in vitro refolding and proteolytic processing. Recombinant tetranectin-as well as natural tetranectin from human plasma-was shown by chemical cross-linking analysis and SDS-PAGE to be a homo-trimer in solution as are other known members of the collectin family of C-type lectins. Biochemical evidence is presented showing that an N-terminal domain encoded within exons 1 and 2 of the tetranectin gene is necessary and sufficient to govern subunit trimerization.

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Amino Acid SequenceBlood ProteinsCloning, MolecularCross-Linking ReagentsEscherichia coliFemaleHumansLectinsLectins, C-TypeMolecular Sequence DataPlacentaPlasminogenPregnancyProtein ConformationProtein FoldingProtein Processing, Post-TranslationalRecombinant Fusion ProteinsSequence Analysis, DNASequence Homology, Amino AcidSolutionsComparative StudyJournal ArticleResearch Support, Non-U.S. Gov't

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T L Holtet, J H Graversen, I Clemmensen, H C Thøgersen, M Etzerodt. 1997. Tetranectin, a trimeric plasminogen-binding C-type lectin.. https://doi.org/10.1002/pro.5560060715

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