| Literature DB >> 7309374 |
Abstract
Avian beta-lipotropin (beta-LPH) was purified from adenohypophyseal glands of the ostrich Struthio camelus by a procedure involving acid/acetone extraction, NaCl fractionation, CM-cellulose chromatography, Sephadex G-75 chromatography and paper electrophoresis (pH 6.7). The 90-amino acid peptide behaved as a single substance during polyacrylamide-gel electrophoresis, isoelectric focusing (pI of 6.0) and N-terminal analysis, the N-terminal amino acid being alanine. Ostrich beta-LPH exhibited lipolytic activity corresponding to an average minimal effective dose of 0.088 micrograms in rabbit adipose tissue.Entities:
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Year: 1981 PMID: 7309374 DOI: 10.1111/j.1399-3011.1981.tb02050.x
Source DB: PubMed Journal: Int J Pept Protein Res ISSN: 0367-8377