Intrinsic inhibitor of inositol 1,4,5-trisphosphate binding.
Rat brain cytosol was applied to a heparin column and eluted with 0.9 M-NaCl. The total binding activity of [3H]inositol 1,4,5-trisphosphate to the eluate was increased about 6-fold compared with the original cytosol. When the eluate was mixed with a flow-through fraction from the heparin column, however, the activity returned to the original level, suggesting that the flow-through fraction contained an inhibitory factor(s) which prevented the binding. The factor(s) was purified by sequential column chromatography using gel permeation, a hydrophobic gel, and finally, a hydroxylapatite gel. Silver staining of sodium dedecyl sulfate gel electrophoresis of the sample thus purified showed a broad band located between the authentic molecular weight markers of 580 and 390 k. A carbohydrate staining method showed that the factor is a glycoprotein.
Hirata
M
M
Department of Biochemistry, Faculty of Dentistry, Kyushu University, Fukuoka, Japan.
Yoshida
M
M
Kanematsu
T
T
Takeuchi
H
H
D000818:Animals; D003600:Cytosol / Q000378:metabolism; D005260:Female; D015544:Inositol 1,4,5-Trisphosphate / Q000037:antagonists & inhibitors* / Q000378:metabolism; D008297:Male; D011485:Protein Binding; D051381:Rats; D017208:Rats, Wistar
D015544:Inositol 1,4,5-Trisphosphate