| pubmed-article:2558658 | pubmed:abstractText | Three distinct ovarian lactogen receptor species with unique and highly reproducible HPLC retention times gave corresponding peaks of binding activity and migrated as single bands of 80, 40, and 34 kDa on SDS-PAGE. Reduction of the 80 kDa protein failed to reveal any conversion to the lower molecular weight proteins by either SDS-PAGE analysis or reverse phase HPLC, suggesting that the three binding proteins are not related by disulfide bond formation. Immunological studies indicate an amino acid homology at a C terminal region among the 3 receptor forms and with the rat liver receptor. However, the 80 kDa ovarian receptor also contains a unique sequence derived from microsequencing that is not immunologically apparent in the ovarian lower molecular weight forms of the rat liver receptor. These findings substantiate the existence of at least two populations of ovarian lactogen receptors perhaps originating within the same gene, a high Mr form potentially capable of signal transduction, and truncated forms that could be involved in transport and/or clearance. | lld:pubmed |
