作者: Georg Reiser
DOI: 10.1016/B978-0-12-185285-6.50030-0
关键词: Chemistry 、 Cerebellum 、 Photoaffinity labeling 、 Biochemistry 、 Cytoplasm 、 Inositol 、 Intracellular 、 Subcellular localization 、 Binding site 、 Receptor
摘要: Publisher Summary This chapter discusses purification of high affinity 1, 3, 4, 5 tetrakisphosphate (IP4) receptor from cerebellum. Membranes pig cerebellum contain high-affinity binding sites for IP4 (KD 1 nM). activity is solubilized using the nonionic detergent Brij 58 and purified by sequential chromatography with CM-cellulose, heparin-agarose, hydroxylapatite. The identified as a 42-kDa protein, this protein established an photoaffinity label. From rat cerebellum, various -binding proteins molecular masses 182 174/84 kDa have been isolated. also takes part in intracellular Ca2+ regulation appears to augment IP3-induced mobilization mouse lacrimal acinar cells. release cerebellar microsomes has found be triggered IP3 IP4. Physiological biochemical experiments indicate that might act concert IP3. contained sample characterized biochemically functionally labeling. provides tools localize cells determine actual functions cellular homeostasis. Subcellular localization may give clues help solve problem whether induces resequestration into internal stores, or regulates entry cytoplasm through plasma membrane.