TEMPERATURE-DEPENDENT NONSPECIFIC ADSORPTION OF RECOMBINANT BOVINE LEUKEMIA-VIRUS RECEPTOR BLVRCP1 IN IMMUNOASSAY

Recombinant bovine leukemia virus receptor, BLVRcp1, possessed the unu sual property of binding plastic plates after blocking nonspecific bin ding sites. Adhesiveness of BLVRcp1 to blocked plates hindered develop ment of an antigen capture and receptor binding assay with this protei n. Unexpectedly, non-specific adsorption of BLVRcp1 was dramatically i nfluenced by temperature. Optimizing incubation temperature and antige n capture at 4 degrees C instead of 37 degrees C and the use of milk a s blocking solution removed nonspecific binding of BLVRcp1 allowing de velopment of a functional immunoassay. Thus, the temperature used for antigen capture can be a critical factor that influences performance o f the immunoassay.