Four avian β‐defensin prepropeptide cDNA sequences [gallinacins: Gal 1 (synonym CHP 1, chicken heterophil peptide 1), and Gal 2; turkey heterophil peptides: THP 1 and THP 2] were amplified from chicken or turkey bone marrow mRNA samples, respectively. Partial chicken β‐defensin cDNA sequences were obtained using degenerate primers based on chicken peptide sequences (Gal 1/CHP 1 and Gal 2). The complete cDNA sequences of the chicken β‐defensins were then determined by designing specific intrapeptidal primers, from the newly acquired sequence, and pairing one primer with a specific poly A primer tail sequence (3′ end) and the other primer with an adapter primer in a 5′ rapid amplification of cDNA ends (RACE) reaction. The two, turkey β‐defensins were amplified from turkey marrow using primers designed from chicken β‐defensin preproregions. The complete amino acid sequences for the prepropeptides were deduced for all four avian β‐defensins. Previously, only partial mature peptide sequences for the turkey β‐defensins and complete mature peptide sequences for the chicken β‐defensins were known. All sequences obtained translated accurately to complete and partial amino acid sequences reported for β‐defensins purified from chicken and turkey heterophil granules except for one additional amino acid for Gal 1/CHP 1. The four deduced β‐defensin proregions lack the long, negatively charged propiece reported in classical defensin proregions. These regions are thought to stabilize and inactivate the positively charged mature peptide and target the propeptide to the storage granule. Instead, these β‐defensin proregions are shorter and similar to storage granule‐free β‐defensins proregions reported for bovine tracheal antimicrobial peptide (TAP) and lingual antimicrobial peptide (LAP). These are the first prepropeptide β‐defensins from leukocyte granules to be completely characterized.