NORMAL MOLECULAR-SIZE OF THE NA+-PHOSPHATE COTRANSPORTER AND NORMAL NA+-DEPENDENT BINDING OF PHOSPHONOFORMIC ACID IN RENAL BRUSH-BORDER MEMBRANES OF X-LINKED HYP MICE

X-linked Hyp mice have a specific defect in Na+-dependent phosphate (Pi) transport at the renal brush border membrane (BBM). In the present study we examined the effect of the Hyp mutation on the molecular size of the Pi transporting unit and on Na+-dependent 14C-phosphonoformic (PFA) binding in renal BBM vesicles. By radiation inactivation analysis, we demonstrated that the molecular size of the Na+-Pi cotransporter is similar in normal (242 ± 16 kDa) and Hyp mice (227 ± 39 kDa). Moreover, while BBM Na+-dependent Pi transport is significantly reduced in Hyp mice (249 ± 54 vs 465 ± 82 pmol/mg protein/6s), genotype differences in (1) Na+-dependent PFA binding (1020 ± 115 vs 1009 ± 97 pmol/mg protein/30 min), (2) Pi-displaceable Na+-dependent PFA binding (605 ± 82 vs 624 ± 65 pmol/mg protein/6s), and (3) phosphate uptake at Na+-equilibrium (67 ± 10 vs 54 ± 7 pmol/mg protein/6s) are not apparent. The present data demonstrate that the molecular size of the renal BBM Na+-Pi cotransporter is normal in Hyp mice and suggest that the number of Na+-Pi cotransporters may not be reduced in the mutant strain. © 1990.