Peptide mapping of multiple forms of cyclic nucleotide phosphodiesterase.

Purified multiple forms of 3':5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) were analyzed using two-dimensional tryptic pep]tide mapping of radioiodinated peptides. Comparisons of peptide maps of rat liver insulin-sensitive phosphodiesterase (PDE) with rat brain calmodulin-sensitive PDE suggest that some peptides co-migrate (31-43% co-migration). However, except for a single peptide, bovine retinal rod outer segment PDE, peptide maps appear unrelated to the other two forms (7-12% co-migration). In contrast, peptide maps of a 36,000-dalton proteolysis product of calmodulin-sensitive PDE are highly related to the peptide maps of a rat brain calmodulin-sensitive holoenzyme (73% co-migration). These results suggest that the multiple PDE forms are distinct molecular entities.