| Literature DB >> 6816630 |
K L Hsi, N G Seidah, G De Serres, M Chrétien.
Abstract
An Mr 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%).Entities:
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Year: 1982 PMID： 6816630 DOI： 10.1016/0014-5793(82)81055-7
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124