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The precursor of recombinant human insulin is also called recombinant proinsulin.It is a fusion protein containing protection peptide and insulin.The protection peptide contains 55 amino acids (48 amino acids from human growth hormone,and a connecting peptide containing Arg-residues) and can effectively improve protein stability and expression efficiency [1].However,in clinical trials the presence of proinsulin in the insulin final products was found to have a negative effect on the heart,leading to an increased incidence of myocardial infarction [2-6].More importantly,recombinant proinsulin is a heterologous protein.Therefore,the removal of the recombinant proinsulin in the final product of insulin is vital,and the effectiveness of its removal should be analyzed by appropriate methods.In this study,we prepared specific monoclonal and polyclonal antibodies against proinsulin and established enzyme-linked immunosorbent assay (ELISA) for the detection of the residual precursor in the insulin production.