Lopap, a prothrombin activator from Lonomia obliqua belonging to the lipocalin family: recombinant production, biochemical characterization and structure-function insights.

Abstract

Using a cDNA library made from Lonomia obliqua caterpillar bristles, we identified a transcript with a 603 bp open reading frame. The deduced protein corresponds to Lopap, a prothrombin activator previously isolated by our group from the bristles of this species. The mature protein is composed by 185 amino acids and shares similarity with members of the… (More)

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Cite this paper

@article{Reis2006LopapAP, title={Lopap, a prothrombin activator from Lonomia obliqua belonging to the lipocalin family: recombinant production, biochemical characterization and structure-function insights.}, author={Cleyson Valença Reis and Sonia Aparecida de Andrade and Oscar Henrique Pereira Ramos and Celso Ra{\'u}l Romero Ramos and Paulo Lee Ho and Isabel de F{\'a}tima Correia Batista and Ana Marisa Chudzinski-Tavassi}, journal={The Biochemical journal}, year={2006}, volume={398 2}, pages={295-302} }