Abstract
Two γ‐LPH variants have been isolated from ostrich pituitary glands using acid acetone extraction, salt fractionation, ion exchange and gel permeation chromatography and HPLC. The two fractions appeared homogeneous on PAG‐IEF (pI = 4.7) and both displayed an alanine N‐terminal residue. Amino acid composition and fragmentation data for these two peptides are in agreement with that expected for the N‐terminal 44 and 46 amino acid residues in ostrich β‐LPH, with corresponding molecular masses of 4911 and 5154 respectively. The molecular mass of the smaller variant was confirmed by means of sedimentation equilibrium centrifugation to be 4717. The two variants displayed lower lipolytic potencies than the corresponding peptides from other species.
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