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1. A 'P2' membrane fraction of bovine tracheal smooth muscle displays high affinity (KD 3.8 +/- 0.2 nM), saturable (Bmax 1003 +/- 170 fmol mg-1 protein) and reversible binding of D-myo[3H]-inositol 1,4,5-trisphosphate ([3H]-Ins(1,4,5)P3). 2. This binding site shows strict stereo- and positional specificity for the D-Ins(1,4,5)P3 isomer with L-Ins(1,4,5)P3, DL-Ins(1,3,4,5)P4 and D-Ins(1,3,4)P3 displacing [3H]-Ins(1,4,5)P3 with Ki values of 20 microM, 0.35 microM and 2.4 microM, respectively. 3. Specific binding of [3H]-Ins(1,4,5)P3 is enhanced at alkaline pH values (maximal at pH 7.75) and, in distinct contrast to [3H]-Ins(1,4,5)P3 binding in rat cerebellum membranes, is not inhibited by Ca2+ (5-500 microM). 4. Heparin displaces [3H]-Ins(1,4,5)P3 specific binding with an IC50 of 7.6 +/- 1.0 micrograms ml-1. 5. Comparative studies demonstrated specific [3H]-Ins(1,4,5)P3 binding in bovine cardiac atrial preparations (Bmax 75 +/- 5 fmol mg-1 protein) and very low specific [3H]-Ins(1,4,5)P3 binding in bovine cardiac ventricle and skeletal muscle membranes (less than or equal to 25 fmol mg-1 protein).

Type

Journal article

Journal

Br J Pharmacol

Publication Date

02/1990

Volume

99

Pages

297 - 302

Keywords

Animals, Binding Sites, Calcium, Calcium Channels, Cattle, Cerebellum, Hydrogen-Ion Concentration, In Vitro Techniques, Inositol 1,4,5-Trisphosphate, Inositol 1,4,5-Trisphosphate Receptors, Kinetics, Male, Membranes, Muscle, Smooth, Rats, Rats, Inbred Strains, Receptors, Cell Surface, Receptors, Cytoplasmic and Nuclear, Stereoisomerism, Trachea