Identical precursors for serum transferrin and egg white conalbumin.

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

Research output: Contribution to journalArticle

94 Citations (Scopus)

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
Externally publishedYes

Fingerprint

Conalbumin
Egg White
Transferrin
Serum
Amino Acids
Cell-Free System
Reticulocytes
Methionine
Chickens
Rabbits
Degradation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Identical precursors for serum transferrin and egg white conalbumin. / Thibodeau, Stephen N; Lee, D. C.; Palmiter, R. D.

In: Journal of Biological Chemistry, Vol. 253, No. 11, 10.06.1978, p. 3771-3774.

Research output: Contribution to journalArticle

Thibodeau, Stephen N ; Lee, D. C. ; Palmiter, R. D. / Identical precursors for serum transferrin and egg white conalbumin. In: Journal of Biological Chemistry. 1978 ; Vol. 253, No. 11. pp. 3771-3774.
@article{a731b05c3c64457cb4f1aec0f2b914b6,
title = "Identical precursors for serum transferrin and egg white conalbumin.",
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.",
author = "Thibodeau, {Stephen N} and Lee, {D. C.} and Palmiter, {R. D.}",
year = "1978",
month = "6",
day = "10",
language = "English (US)",
volume = "253",
pages = "3771--3774",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "11",

}

TY - JOUR

T1 - Identical precursors for serum transferrin and egg white conalbumin.

AU - Thibodeau, Stephen N

AU - Lee, D. C.

AU - Palmiter, R. D.

PY - 1978/6/10

Y1 - 1978/6/10

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0018265043&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0018265043&partnerID=8YFLogxK

M3 - Article

C2 - 649604

AN - SCOPUS:0018265043

VL - 253

SP - 3771

EP - 3774

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 11

ER -