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.
Sawitzke
A L
AL
Department of Physiology, University of Utah School of Medicine, Salt Lake City 84132.
Griffin
J
J
Odell
W D
WD
D015153:Blotting, Western; D006063:Chorionic Gonadotropin; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004340:Drug Contamination; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D015592:Immunoradiometric Assay; D007986:Luteinizing Hormone / Q000302:isolation & purification*; D011863:Radioimmunoassay / Q000379:methods
D006063:Chorionic Gonadotropin; D007986:Luteinizing Hormone