Differently glycosylated multiple forms of renin in the blood circulation of rats.

Serial lectin chromatography of rat plasma on concanavalin A and lentil lectin columns separated plasma renin into differently glycosylated multiple forms. To study the role of glycosylation in the clearance of circulating renin, three different forms of glycosylated renin (renin A, B-1 and B-2) were highly purified from rat kidneys. Renin A and B-1 were loosely and tightly, respectively, bound to concanavalin A, but did not bind to lentil lectin. Renin B-2 was bound to both concanavalin A and lentil lectin. Each form of renal renin, labelled with 125I and intravenously given to rats, disappeared from the blood circulation at different rates, and distributed in the liver and kidney to different extents. Deglycosylation of renin B-1 with endoglycosidase F led to reduced metabolic clearance rates and to a significant decrease in uptake by the liver. These results show the heterogeneity in the fate of circulating renin due to the heterogeneity of glycosylation.