Isolation and NH2‐terminal sequence of a novel porcine anterior pituitary polypeptide
Open Access
- 18 October 1982
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 147 (2) , 261-266
- https://doi.org/10.1016/0014-5793(82)81055-7
Abstract
An M r 21 000 polypeptide, designated APPG, has been purified by reverse‐phase, high‐performance liquid chromatography (RP‐HPLC), from acid extracts of porcine anterior pituitary glands. This acidic protein possesses an isoelectric point of 4.9. Amino acid analysis shows that it is not a glycoprotein and estimates it to contain about 173 amino acids. NH2‐terminal sequence analysis allowed the determination of the first 50 residues unambiguously. A computer data bank search using a mutation data matrix and comparison with 269 012 protein segments indicated that this is a novel polypeptide sequence. However, this search revealed suggestive sequence homologies to a number of peptides of known sequence, including duck proinsulin (30%), Rous sarcoma virus transforming protein TVFV60 (24%) and pig secretin (26%).Keywords
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