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Horm Metab Res 1977; 9(4): 294-299
DOI: 10.1055/s-0028-1093516
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© Georg Thieme Verlag KG Stuttgart · New York

The Purification and Characterization of a Lipolytic Factor From Bovine Pituitaries

S.  Assa [*] , Z.  Laron [**]
  • Institute of Pediatric and Adolescent Endocrinology, Beilinson Hospital, Petah Tikva and Sackler School of Medicine, Tel Aviv University, Israel
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Publication History

Publication Date:
23 December 2008 (online)

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Abstract

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 10-9mMol/ml. An immunological cross reaction was found between BLF and anti luteinizing hormone β chain. This can denote that BLF and LH β chain share similar or identical immunological determinants. The possibility is raised that LH β chain is the precursor of BLF.

Key words

Growth Hormone - Bovine Lipolytic Factor (BLF)

1 In partial fulfillment for the requirements of a Ph.D. degree of Tel Aviv University School of Medicine, Israel.

2 Established Investigator of the Chief Scientist's Bureau, Ministry of Health.

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