Amino-terminal sequence of chicken preproalbumin.

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 translocation product (preproalbumin) contains an NH2-terminal extension of 18 amino acid residues. The NH2-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-Arg1, where Arg1 represents the NH2-terminal residue of proalbumin. This NH2-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.