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Nucleotide sequence analysis of cDNAs encoding a bovine galanin precursor protein in the adrenal medulla and chemical isolation of bovine gut galanin
Author(s) -
Rökaeus Åke,
Carlquist Mats
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80125-x
Subject(s) - galanin , amino acid , peptide sequence , complementary dna , biology , adrenal medulla , biochemistry , nucleic acid sequence , protein primary structure , microbiology and biotechnology , methionine , peptide , gene , neuropeptide , endocrinology , catecholamine , receptor
A description is given of the primary structure of a bovine adrenal medullary precursor protein (123 amino acids), containing a nonrepetitive galanin sequence, different in four amino acid positions from pig galanin, structural information deduced from the nucleotide sequence analysis of two cDNA clones. Pairs of lysine and arginine residues separate the galanin sequence N‐terminally from the initiating methionine and a 29 amino acid leader peptide and C‐terminally from a 59 amino acid peptide. The deduced amino acid composition was confirmed by the isolation and determination of the amino acid composition for bovine intestinal galanin. Northern blot analysis revealed the presence of an apparent single galanin mRNA species, of approx. 850–900 bases in size, which was present in a population of chromaffin cells scattered throughout the bovine adrenal medulla.