Bovine globin has been incubated with mice peritoneal macrophages in o
rder to study its hydrolysis by lysosomal enzymes, among which chiefly
cathepsin D. Analysis of resulting peptides, by reversed-phase high-p
erformance liquid chromatography (RP-HPLC), shown the release of a bio
active peptide, VV-hemorphin-7. When a carboxyl proteinase inhibitor s
uch as pepstatin A was added, no hemorphin was generated, Our results
clearly demonstrated that VV-hemorphin-7 generation was principally du
e to cathepsin D. This study allowed us to hypothetize a possible path
way for in vivo hemorphins appearance from globin catabolism by macrop
hages.