A number of ABO grouping, Rh typing, antibody screening, and antibody identification problems are associated with chemicals in blood bank reagents. We describe a newly discovered agglutination phenomenon due to a thimerosal (Merthiolate)-dependent agglutinin found in the serum of a normal blood donor. Thimerosal is used as a preservative in several low-ionic strength reagents. This agglutination phenomenon is detected only in test systems (low-ionic-strength, albumin, saline, ficin treated test cells) in which test cells are incubated in the presence of thimerosal. Agglutination does not occur in the absence of thimerosal. The thimerosal-dependent agglutinin behaves like an IgG IgG autoantibody. There is no evidence that the thimerosal-dependent agglutinin is responsible for increased red cell destruction.

Results show that bactericidal activity of bovine and porcine AM was enhanced by tilmicosin, but not in proportion to the reported ability of AM to concentrate tilmicosin intracellularly. With or without exposure to tilmicosin, the time-course of bactericidal activity of bovine AM against M haemolytica and of porcine AM against A pleuropneumoniae or P multocida was too complex to be reduced to a simple linear equation.

Two low ionic strength-dependent autoagglutinins were studied and found to have anti-Pr(1) specificity. This specificity was determined by studies with enzyme-treated and neuraminidase-treated human red blood cells (RBCs), animal RBCs and chemically-modified sialoglycoproteins, all suspended in a low ionic strength solution (LISS). Both IgM complement-binding cold agglutinins had a wide thermal range and caused in vitro hemolysis of some LISS-suspended RBCs at 37°C. Compatible blood was found for these patients by using techniques that did not employ LISS.

Two low ionic strength-dependent autoagglutinins were studied and found to have anti-Pr1 specificity. This specificity was determined by studies with enzyme-treated and neuraminidase-treated human red blood cells (RBCs), animal RBCs and chemically-modified sialoglycoproteins, all suspended in a low ionic strength solution (LISS). Both IgM complement-binding cold agglutinins had a wide thermal range and caused in vitro hemolysis of some LISS-suspended RBCs at 37 degrees C. Compatible blood was found for these patients by using techniques that did not employ LISS.