A gene for G protein from Streptococcus strain G148 was cloned in Escherichia coli, which gave rise to several plasmids. One plasmid containing a 1.5 kb insert coding for entire G protein with 63 kD. This protein had both an IgG binding capacity and albumin-binding activity. The second plasmid containing a 0.7 kD insert coded for protein with MM of 38 kD and had only an IgG-binding activity. The third coding for protein with 25 kD has only albumin-binding activity. After subcloning the 1.5-kb insert into the other vector pSP65 and analysing the nucleotide sequence of this insert both in pSP65 vector, the authors came to the conclusion that the proteins obtained are fusion protein of G protein and beta-galactosidase. All the proteins were prepared by affinity chromatography on IgG sepharose or on HSA sepharose. The interaction between G protein and polyclonal and monoclonal IgG of the reactions between G protein and human IgG have determined.