Isolation and NH2-terminal sequence of a novel porcine anterior pituitary polypeptide. Homology to proinsulin, secretin and Rous sarcoma virus transforming protein TVFV60

FEBS Lett. 1982 Oct 18;147(2):261-6. doi: 10.1016/0014-5793(82)81055-7.

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%).

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Chromatography, High Pressure Liquid
  • Molecular Weight
  • Oncogene Protein pp60(v-src)
  • Peptides / isolation & purification*
  • Pituitary Gland, Anterior / analysis*
  • Proinsulin / analysis
  • Secretin / analysis
  • Viral Proteins / analysis

Substances

  • Peptides
  • Viral Proteins
  • Secretin
  • Proinsulin
  • Oncogene Protein pp60(v-src)