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Purified preparations of human luteinizing hormone are contaminated with small amounts of a chorionic gonadotropin-like material.

We have identified a CG-like protein contaminating a purified human LH preparation of immunochemical grade. This CG-like material is estimated to comprise 0.17%, by weight, of the LH and reacts in specific, sequential-type, two-monoclonal antibody, immunoradiometric assays for CG as well as in the carboxyl-tail CG RIA. The CG-like material is not separable from LH by size exclusion or ion exchange chromatography. The LH can be freed of this small contamination of CG-like material by immunopurification employing specific monoclonal antibodies. Sephadex G-100 chromatography shows this material to have a mol wt of 40.0K. Western blot analysis of the LH run under nonreducing conditions, using an anti-CG carboxyl-tail primary antibody, reveals two bands of this CG-like material, one at 60.8K and one at 50.7K. When electrophoresed under reducing conditions, the material reacts with the anti-CG carboxyl-tail antibody at several mol wt, ranging from 10.5-64K.