In a denaturing polyacrylamide gel electrophoresis (PAGE) experiment, pure intact adult human hemoglobin is expected to separate based on the polypeptide chains it contains. Human hemoglobin primarily consists of two types of polypeptide chains: the alpha (α) and beta (β) chains, typically forming a tetrameric structure with the formula α2β2. When subjected to denaturing PAGE, which disrupts the non-covalent interactions and secondary structure, each distinct type of chain should result in a separate band. Thus, we expect two distinct bands: one for the α chains and one for the β chains. Therefore, in such an experiment, pure intact adult human hemoglobin typically yields 2 bands.