(3, is a highly reactive, mechanism-based inhibitor of serine proteases. We show here that glycogeu phosphorylase b is also inactivated by this inhibitor, in a mechanism that parallels the in~tivation of serine proteases, but involving multiple sites of covalent modification. Such a process may compromise studies in which 3,4-DC1 is used to arrest proteolysis of a second native protein which may itself be modified.3,4-Dichloroisoeoumarin; Glycogen phosphorylase 1,