Appelgren L E, Odlind B, Wistrand P J
Department of Pharmacology and Toxicology, Swedish University of Agricultural Sciences, Uppsala.
Acta Physiol Scand. 1989 Nov;137(3):449-56. doi: 10.1111/j.1748-1716.1989.tb08776.x.
Carbonic anhydrase (CA) isozymes CA I and CA II were isolated from rat erythrocytes, and CA III from rat skeletal muscle. They were purified to homogeneity and labelled with 125I using the Bolton-Hunter method. The tissue distribution of these [125I]CA isozymes was studied in rats with whole-body autoradiography at various times after an intravenous injection. The distribution pattern showed a remarkable organ specificity. CA I and CA III were to a great extent localized to the renal cortex. This is compatible with renal uptake, secondary to glomerular filtration, of these isozymes. This would be expected from the renal handling of proteins with the following characteristics: molecular weight of 29,000; iso-electric points, pI, around 7.2 and 6.5 respectively. However, CA II of similar molecular shape and size, with a pI of 6.8, remained in the blood and was preferentially localized to the liver. Further studies are needed to clarify why such similar proteins are targeted to different organs.