Purification of bovine cholecystokinin-58 and sequencing of its N-terminus

John Eng, Han Rui Li, Rosalyn S. Yalow

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Molecular cloning of cholecystokinin (CCK) mRNA from porcine brain and gut has demonstrated that CCK is synthesized as an identical precursor in both tissues. The sequence for porcine CCK-58 predicted from CCK cDNA was identical with the amino acid sequence of the peptide purified from different lots of animals. However one group did report that there were differences in the N-terminus of CCK-58 purified from the intestines of two different lots of mongrel dogs. In the current report it is demonstrated that the amino acid sequences of CCK-58 purified separately from three bovine brains are identical through the first 19 N-terminal amino acid residues. The peptides were sequenced for ten additional steps and were shown to be identical with the previously reported sequences for the N-terminus of CCK-39. The N-terminus of bovine CCK-58 has the following sequence: AVPRVDDEPRAQLGALLAR.

Original languageEnglish
Pages (from-to)15-19
Number of pages5
JournalRegulatory Peptides
Volume30
Issue number1
DOIs
StatePublished - 21 Aug 1990
Externally publishedYes

Keywords

  • Amino acid sequence
  • CCK-58, N-terminus (bovine)
  • Peptide purification

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