Vahid Jalali Javaran1, Alireza Shafeinia1, Mokhtar Jalali Javaran2, Esmaeil Ghasemi Gojani1, Malihe Mirzaee3. 1. Department of Biotechnology, Ramin University of Agriculture and Natural Resources, Ahwaz, 63417-711, Iran. 2. Department of Biotechnology, Tarbiat Modares University, Tehran, 14115-336, Iran. M_jalali@modares.ac.ir. 3. Department of Biotechnology, Tarbiat Modares University, Tehran, 14115-336, Iran.
Abstract
OBJECTIVE: To use a transient expression system to express a truncated human tissue plasminogen activator (K2S) gene in cucurbit plants. RESULTS: The recombinant tissue plasminogen activator protein (K2S form) was expressed in active form in cucurbit plants. Its molecular weight was 43 kDa. The plant-derived rt-PA was determined using goat anti-rabbit antibody by western blotting. Among the infected lines, the highest expression of rt-PA was 62 ng/100 mg per leaf tissue as measured by ELISA. The enzymatic activity of the plant-derived rt-PA was 0.8 IU/ml. CONCLUSIONS: The K25 form of rt-PA was expressed for the first time using the viral expression system. Plant-derived rt-PA showed similar potency to commercially-available PA.
OBJECTIVE: To use a transient expression system to express a truncated humantissue plasminogen activator (K2S) gene in cucurbit plants. RESULTS: The recombinant tissue plasminogen activator protein (K2S form) was expressed in active form in cucurbit plants. Its molecular weight was 43 kDa. The plant-derived rt-PA was determined using goat anti-rabbit antibody by western blotting. Among the infected lines, the highest expression of rt-PA was 62 ng/100 mg per leaf tissue as measured by ELISA. The enzymatic activity of the plant-derived rt-PA was 0.8 IU/ml. CONCLUSIONS: The K25 form of rt-PA was expressed for the first time using the viral expression system. Plant-derived rt-PA showed similar potency to commercially-available PA.