Open AccessAmino‐Terminal Sequence of Chicken Preproalbumin
Author(s) -
COMPERE Sally J.,
LIVELY Mark O.,
MacGILLIVRAY Ross T. A.
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb05354.x
Subject(s) - edman degradation , amino acid , reticulocyte , peptide sequence , biochemistry , signal peptide , biology , homology (biology) , microbiology and biotechnology , chemistry , rna , gene
Poly(A)‐containing RNA was isolated from chicken liver and translated in a reticulocyte lysate protein‐synthesizing system in the presence of radiolabeled amino acids. Chicken albumin was isolated from the translation products by immunoprecipitation, and subjected to automated Edman radiosequencing. Comparison with the sequence of proalbumin showed that the translation product (preproalbumin) contains an NH 2 ‐terminal extension of 18 amino acid residues. The NH 2 ‐terminal sequence of chicken preproalbumin was as follows: Met −18 ‐Lys‐Asn‐Val −15 ‐Thr‐Leu‐Ile‐Ser‐Phe −10 ‐Ile‐Phe‐Leu‐Phe‐Ser −5 ‐Ser‐Ala‐Thr‐Ser −1 ‐Arg 1 , where Arg 1 represents the NH 2 ‐terminal residue of proalbumin. This NH 2 ‐terminal extension is very rich in hydrophobic amino acid residues and is similar to the signal sequences found in other secreted proteins. The signal sequence of chicken preproalbumin shows considerable homology with the signal sequences of rat and bovine preproalbumins, but little homology with the signal sequences of other chicken preproteins.