Identical precursors for serum transferrin and egg white conalbumin.

S. N. Thibodeau, D. C. Lee, R. D. Palmiter

Research output: Contribution to journalArticle

94 Scopus citations

Abstract

The NH2-terminal sequences of egg white conalbumin and chicken serum transferrin were examined and found to be identical. Conalbumin, when synthesized in a rabbit reticulocyte cell-free translation system, was found to contain an NH2-terminal extension of 19 amino acid residues. Sequential Edman degradation of this precursor (pre-conalbumin) labeled with radioactive amino acids revealed the following sequence: formula see text: The vertical line indicates the site at which pre-conalbumin is cleaved to yield authentic conalbumin. The sequence represents the primary translation product since the NH2-terminal methionine was shown to be derived from initiator Met-tRNAfMet. A partial NH2-terminal sequence of transferrin synthesized in vitro was also determined (underlined residues) and it is identical with that of pre-conalbumin.

Original languageEnglish (US)
Pages (from-to)3771-3774
Number of pages4
JournalJournal of Biological Chemistry
Volume253
Issue number11
StatePublished - Jun 10 1978

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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