Effects of trifluoperazine, a calmodulin antagonist, on rabbit T- and B-cell responses to mitogens and antigen.

Trifluoperazine (TFP), an inhibitor of the calcium-binding protein, calmodulin (CaM), was used to assess the role of calmodulin in the responses of rabbit lymphoid cells to stimulation with mitogen and antigen. After binding goat anti-rabbit Fab antibody, rabbit B cells lose their surface immunoglobulin (Ig) through endocytosis and then reexpress this protein during the next 24 hr. This reexpression was markedly inhibited by TFP.

Absence of phospholipase activity in bacteriophage T4.

We assayed phospholipase activity in T4Dt+ and in t mutant phage grown under permissive and restrictive conditions. There was no correlation between the presence of the t+ gene product and phospholipase activity. Phospholipase activity in phage lysates could be attributed to the presence of bacterial debris or to the use of commercial DNase which contains phospholipase.

Isolation and mapping of t gene mutants of bacteriophage T4D.

A procedure for selective isolation of T4 t mutants is described. At 120 min after infection of Escherichia coli cells with a low multiplicity of T4 bacteriophage, the mixture was sedimented through a linear sucrose gradient, and infected cells that remained intact were collected as the fastest sedimenting fraction. Ten to 50% of the phage released by chloroform treatment of this fraction were t mutants.

Cadaverine in bacteriophage T4.

Cadaverine was found in bacteriophage T4 when the host cells of Escherichia coli K-12 were grown in complex media and aerated by agitation. Only traces of cadaverine were found if the host was grown and agitated in synthetic medium or was aerated by vigorous bubbling in a complex medium. When the host cells were grown anaerobically in a complex medium, cadaverine became the major polyamine in the progeny phage.