Purification and characterization of porcine prorelaxin |
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| Institution: | 1. Department of Intensive Care Unit Affiliated Hospital of Binzhou Medical University, Binzhou 256603, Shandong Province, China;2. Department of Intensive Care Unit, Hulunbeier People''s Hospital, Hulunbeier 021000, Inner Mongolia Autonomous Region, China;3. Department of Respiratory Medicine, Affiliated Hospital of Binzhou Medical University, Binzhou 256603, Shandong Province, China;4. Department of Biotechnology, Binzhou Medical University, Yantai 264003, Shandong Province, China;5. Department of Cell Biology, Binzhou Medical University, Yantai 264003, Shandong Province, China |
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| Abstract: | Relaxin is a two-chain 6-kDa peptide hormone. It is a member of the insulin family of peptides and is produced mainly during pregnancy to prepare the reproductive tract for birth. In the pig, relaxin is produced mainly by ovarian luteal cells. It is processed via the regulated pathway from a larger (18 kDa) precursor, prorelaxin. Protocols have been described for the purification of mature relaxin from the ovaries of pregnant gilts. Multiple forms of relaxin have been detected during isolation due to exopeptidase trimming of the peptide chains. To date, such trimming events have prevented purification of the larger relaxin precursor. Described here is a method for the isolation of milligram amounts of homogeneous and bioactive prorelaxin from porcine ovaries. |
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