Transblot identification of avidin-interacting proteins in rat salivary glands

Blotting of rat parotid gland proteins separated by SDS-PAGE and transferred to Immobilon transfer membranes revealed that avidin-peroxidase conjugate interacted with bands having estimated molecular weights of 72, 74, and 120 kDa. Even at the lowest concentration of avidin-peroxidase used in the general ABC method (1:2000 dilution), three bands were clearly discernible. The staining reaction of parotid gland proteins was eliminated on preincubating the proteins with native avidin. The staining reaction was markedly reduced with the proteins obtained from submandibular/sublingual glands.