Expression and purification of kringle domains of human apolipoprotein (a) in E. coli

摘要

Methods for the expression of kringle domains of apoliprotein(a) are described. The domains, including kringle 4 domains and the unique kringle 5 domain, are efficiently expressed as fusion proteins from transformed Escherichia coli host cells. The fusion polypeptides may be employed directly to generate antibodies to human lipoprotein (a) or cleaved to provide the pure kringle polypeptide. Monoclonal antibodies to the kringle 4 domains and to kringle 5 domain may be employed to assay levels of human apolipoprotein (a) in blood as a measure of risk of coronary heart disease.