The purification and characterization of a lipolytic factor from bovine pituitaries.

During the purification of a bovine growth hormone preparation (S408A) a yet unknown lipolytic peptide as obtained. This substance was subjected to CM cellulose chromatography followed by differential precipitation with trichloracetic acid. The resulting purified peptide was homogenous on disk electrophoresis and consisted of 36 amino acids with a molecular weight of 4.000. The lipolytic activity was found to be very high and 20-fold that of the starting material, Protein recovery was 1.8%. This peptide, called bovine pituitary lipolytic factor (BLF) was active in rat adipose tissue, exhibiting a minimal effective dose (MED) of 0.05 x 10(-9) mMol/ml. An immunological cross reaction was found between BLF and anti luteinizing hormone beta chain. This can denote that BLF and LH beta chain share similar or identical immunological determinants. The possibility is raised that LH beta chain is precursor of BLF.