Tissue homogenates from rainbow trout gill had three- to fivefold higher specific activity for 5'-nucleotidase (5'NT) and more than twofold greater alkaline phosphodiesterase (APD) activity than liver or kidney homogenates. In isolated plasma membranes, gill 5'NT activity was 3-5 times greater than that of the kidney or liver; gill and kidney plasma membranes had similar APD specific activities, both more than five times that of liver. 5'NT and APD activities were localized by histochemistry to the endothelial (pillar) cells of trout gill secondary lamellae. Staining was consistent with the concentration of both activities at the apical plasma membranes of pillar cells (i.e. at the lamellar microvascular surfaces). This localization may reflect a capacity for processing nucleotide metabolites circulating in the blood, perhaps relating to purinergic regulation of local lamellar hemodynamics. There was no histochemical evidence of either 5'NT or APD activity in the gill epithelial (pavement) cells that interface directly with the environment. In contrast, in trout kidney, both enzyme activities localized to the apical region of tubule epithelial cells. The absence of 5'NT and APD activity in pavement cells reinforces the unique structural and functional character of the gill-environment epithelial barrier. The results indicate that 5'NT and APD activities have particular potential application as markers in efforts to isolate and characterize specific gill plasma membrane fractions.
Biochemical and histochemical evidence for stimulation of myosin ATPase activity in thyrotoxic rabbit heart
