A NEW REAGENT FOR THE GUANIDINATION OF PROTEINS

Abstract
A reagent, 1-guanyl-3,5-dimethyl pyrazole nitrate, has been used for the guanidination of bovine serum albumin and β-lactoglobulin. The reagent is more stable and permits the guanidination to occur under more gentle conditions than the O-methyl isourea formerly employed. The modified albumin had the same sedimentation coefficient and electrophoretic mobility as the native protein. The guanidination of β-lactoglobulin required blocking of the sulphydryl groups by N-ethyl maleimide and iodoacetic acid. Guanidinated β-lactoglobulin had a lower sedimentation coefficient and greater negative electrophoretic mobility than native lactoglobulin.