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

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%).

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Hsi KL,Seidah NG,De Serres G,Chrétien M

doi

10.1016/0014-5793(82)81055-7

subject

Has Abstract

pub_date

1982-10-18 00:00:00

pages

261-6

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(82)81055-7

journal_volume

147

pub_type

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