Luteinizing Hormone (LH) from goat pituitary glands has been purified and characterized with respect to its size and subunit nature. The purification at each step was monitored by protein estimation, SDS-PAGE, and direct binding ELISA. The final product was found to be over 90 fold purified as compared to the starting pituitary extract, and the yield of the final purified LH was found to be 65.3 mg/kilogram of wet pituitary glands. Fractionation of the cLH into different charge isoforms by SP-Sephadex ion exchanger has been observed. Chromatography on immobilized Con A lectin resulted in fractionation of the purified cLH into unbound (2%), loosely bound (85%), and firmly bound (13%) fractions indicating oligosaccharide heterogeneity. The purified hormone was capable of stimulating weight increase in the seminal vesicles in immature male rats, with a biopotency equivalent to the 2200 I.U. of hCG per mg of purified cLH. The FSH content of the purified cLH was found to be less than 0.0165% as indicated by in vivo Steelman-Pohley assay.