We describe here the latest observations on poly(ADP-ribose) glycohydr
olase. There is now extensive evidence that this nuclear enzyme is an
endo-exoglycosidase which has a key role to perform in the removal of
polymers which interact with proteins through covalent and non-covalen
t interactions. Also, we have developed a zymogram which will permit t
he isolation of the various isoforms of the glycohydrolase and the eve
ntual cloning of this enzyme. Finally, we have evidence that very shor
t oligomers and even monomers of ADP-ribose covalently bound to protei
ns can be removed by poly(ADP-ribose) glycohydrolase.