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Am J Physiol Cell Physiol 258: C933-C943, 1990;
0363-6143/90 $5.00
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AJP - Cell Physiology, Vol 258, Issue 5 C933-C943, Copyright © 1990 by American Physiological Society

ARTICLES

Binding of bumetanide to microsomes from optic ganglia of the squid, Loligo pealei

A. A. Altamirano, B. A. Watts 3rd and J. M. Russell
Department of Physiology and Biophysics, University of Texas Medical Branch, Galveston 77550.

Saturable high-affinity binding of [3H] bumetanide [dissociation constant (KD) = 80 nM] was measured in microsomal membranes prepared from squid optic ganglia. Under control conditions, the maximal specific binding of labeled bumetanide (Bmax) was approximately 6-7 pmol/mg protein. Binding had a higher relative affinity for bumetanide than for furosemide and depended on the presence of Cl- and K+, but not Na+, in the incubation media. In the case of K+, [3H]bumetanide binding was half-saturated at [K+] = 100 mM. The Cl- effect was biphasic. At [Cl-] between 0 and 150 mM, [3H]bumetanide binding increased with increasing [Cl-]. However, when [Cl-] was increased above 150 mM, [3H]bumetanide binding was progressively reduced. ATP acted as a nonessential activator [mean affinity constant (K0.5) approximately 1 microM] of the ion-dependent [3H]bumetanide binding by increasing the apparent binding capacity. The activation by ATP did not require Mg2+. Other adenosine analogues also stimulated the binding of bumetanide.


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