Isolation and NH2-terminal sequence of a novel porcine anterior pituitary polypeptide. Homology to proinsulin, secretin and Rous sarcoma virus transforming protein TVFV60.
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%).
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D008970:Molecular Weight; D015688:Oncogene Protein pp60(v-src); D010455:Peptides / Q000302:isolation & purification*; D010903:Pituitary Gland, Anterior / Q000032:analysis*; D011384:Proinsulin / Q000032:analysis; D012633:Secretin / Q000032:analysis; D014764:Viral Proteins / Q000032:analysis
D010455:Peptides; D014764:Viral Proteins; D012633:Secretin; D011384:Proinsulin; D015688:Oncogene Protein pp60(v-src)