The b₂-adrenergic receptor (b₂AR) carries two non- synonymous single nucleotide polymorphisms in its extracellular domain that have been suggested to have an influence on the phenotype of common disorders such as asthma. The b₂ARs are widely studied members of the G protein-coupled receptor family but little is known about their biosynthesis. In this study human b₂AR Gly16Arg variants were investigated in a heterologous expression system. Inducible HEK-293 cell lines stably expressing the variants with an N-terminal Myc-tag and with or without a C-terminal Flag-tag were used. Cell surface expression of the Arg16 variant was lower compared to the Gly16 variant when measured by flow cytometry. By cell surface biotinylation and enzymatic deglycosylation assays, followed by Western blot analysis, two receptor species were identified: a mature cell surface receptor and an intracellular biosynthetic intermediate. Both variants were fairly efficient in maturation as 70–80 % of the newly synthesized receptors were converted to mature receptors studied by pulse-chase labeling. In addition, the two variants behaved similarly in terms of maturation kinetics. However, after longer chase times the Arg16 variant was detected also in smaller molecular weight forms that were absent for the Gly16 variant. They possibly represent proteolytically cleaved fragments. Thus, a single amino acid change from a neutral glysine to a charged arginine in the N-terminal region of the b₂AR seems to decrease the cell surface expression of the receptor. Since no significant differences in maturation were observed, these data indicate faster turnover rate for the Arg16 variant at the cell surface.