七鳃鳗组织蛋白酶D成熟肽结构域的原核表达及功能研究

athepsin D (cathepsin D, CTSD) is a lysosomal aspartic acid protease, and is related to the various processes of protein hydrolysis, which plays important roles in immune response and digestion process of vertebrates. Lampreys are one of the most primitive vertebrates, and have been considered as the ideal animal models to study the origin and evolution of vertebrates. In order to study the biological functions of lamprey cathepsin D, the mature domain of lamprey cathepsin D without the signal peptide and prepeptide was subcloned into pCold I vector, and expressed in the Rosseta blue induced with IPTG. After renaturation of inclusion body, the soluble mature domain of lamprey cathepsin D was obtained eventually. And the mature domain was able to hydrolyze bovine hemoglobin. The successful expression of lamprey cathepsin D mature domain provides much information for the further studies of biological functions of lamprey cathepsin D.