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PMID: 721826 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Precursor of egg white ovomucoid. Amino acid sequence of an NH2-terminal extension.

The Journal of biological chemistry ·Vol. 253 ·No. 24 ·1978-12-25 ·Pages 9018-23

Thibodeau SN, Palmiter RD, Walsh KA

Abstract

The translation of ovomucoid mRNA in a reticulocyte lysate protein-synthesizing system yields a precursor form which contains an NH2-terminal extension of 23 amino acid residues. Edman degradation of radioactive translation products (pre-ovomucoid) identified the following sequence: formula : (see text), where the initiator methionine (in parentheses) is the only residue cleaved from the NH2 terminus during cell-free synthesis and the vertical line indicates the site at which pre-ovomucoid is cleaved in vivo to yield ovomucoid. The precursor sequence differs from those of two other proteins (pre-lysozyme and pre-conalbumin) secreted by the same cell, but resembles these and other secretory protein "signal peptides" in both length and hydrophobicity. Pre-ovomucoid does not interact with trypsin in the same manner as mature ovomucoid.

MeSH Terms
Amino Acid Sequence Animals Chickens Egg Proteins/biosynthesis Egg White Oviducts/metabolism Ovomucin/biosynthesis Precipitin Tests Protein Biosynthesis RNA, Messenger/metabolism Rabbits Reticulocytes/metabolism
Chemicals
Egg Proteins RNA, Messenger Ovomucin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Thibodeau S N
Palmiter R D
Walsh K A
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1978-12-25
Pages
9018-23
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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