Isolation and NH2‐terminal sequence of a novel porcine anterior pituitary polypeptide

FEBS Letters

De Serres, G.¹  Chrétien, M.¹  Hsi, K.L.¹  Seidah, N.G.¹ 

[1] Clinical Research Institute of Montreal, 110 Pine Avenue West, Montreal H2W 1R7, Canada

关键词: Anterior pituitary peptide sequence;    Proinsulin;    Secretin;    Rous sarcoma virus transforming protein;   

DOI  :  10.1016/0014-5793(82)81055-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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%).

【 授权许可】

Unknown