Post-translational processing of preprotachykinins. Isolation of protachykinin-(1-37)-peptide from human adrenal-medullary phaeochromocytoma tissue

R. Kage, L. Thim, W. Creutzfeldt, J. M. Conlon

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

Abstract

The biosynthetic precursors of the mammalian tachykinins, α-, β- and γ-preprotachykinins, contain a common N-terminal region of 74 amino acids. A polyclonal antiserum was raised against a synthetic peptide representing N-tyrosylated β-preprotachykinin-(48-56)-peptide as predicted from the nucleotide sequence of cloned DNA complementary to human β-preprotachykinin mRNA. By using this antiserum in radioimmunoassay, a single immunoreactive peptide was identified in an extract of a human pheochromocytoma that produced substance P and neurokinin A. Partial microsequencing and determination of the amino acid composition of the peptide indicated identity with preprotachykinin-(20-56)-peptide. Thus the data demonstrate that the Ala19-Glu20 bond in preprotachykinin is the site of cleavage of the signal peptide.

Original languageEnglish
Pages (from-to)203-207
Number of pages5
JournalBiochemical Journal
Volume253
Issue number1
DOIs
Publication statusPublished - 1988
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Post-translational processing of preprotachykinins. Isolation of protachykinin-(1-37)-peptide from human adrenal-medullary phaeochromocytoma tissue'. Together they form a unique fingerprint.

Cite this