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Mouse prolactin (mPRL) is a single-chain polypeptide hormone, with a molecular weight of 23kDa, containing 197 amino acid residues, and it is secreted from the prolactin cells of the anterior pituitary gland. Prolactin (PRL) exhibits a wide variety of activities in vertebrates, including growth and differentiation of mammary epithelium, lactation, osmoregulation and parental behavior in teleosts, amphibian development, broodiness in hens and production of crop sac 'milk' in pigeons1,5,7,8). Measurements of serum level of mPRL as well as those of other hormones in order to study the physiological role of hormones require the methods of high sensitivity and specificity, and homologous radioimmunoassay (RIA) for mPRL has previously been established as an accurate assay4,6). However, RIAs are becoming unsuitable because of concerns related to the handling of radioactive materials and the elimination of radioactive wastes, and it is impossible to perform an experiment without the RI facility. From these reasons, enzyme-linked immunosorbent assay (ELISA) has been recently developed for measurement of hormones using an enzyme in place of the radioisotope and this method provide a safety handling and considerable accuracy and sensitivity of assay10). The recombinant mPRL (met-mPRL) has been produced in E. coli cells by recently developed recombinant DNA techinques13). The cDNA for mPRL, which was cloned and sequenced previously by HARIGAYA et al.3), has been modified and reconstructed in an expression vector plasmid. The recombinant plasmid was used for production of recombinant mPRL in E. coli cells. The expressed met-mPRL had a molecular weight of 23kDa and possessed biological activity comparable to that of natural pituitary PRL. The aim of the present study was to develop a noncompetitive enzyme-linked immunosorbent assay for mPRL using this recombinant mPRL expressed in E. coli cells.

An Enzyme Immunoassay for the Determination of Serum Prolactin in Mice: Developed by Recombinant Mouse Prolactin