Malamud D F, DiRusso C C, Aprille J R
Biochim Biophys Acta. 1977 Nov 23;485(1):243-7. doi: 10.1016/0005-2744(77)90211-x.
Mn2+-stimulated adenylate cyclase (ATP pyrophosphate-lyase-(cyclizing), EC 4.6.1.1) activity in detergent solubilized preparations from mouse brain. While NaF-stimulated activity was decreased by both solubilization and storage at 0--4 degrees C, the ability of the enzyme to be stimulated by Mn2+ was maintained for up to one week. By including Mn2+ in the assay of adenylate cyclase in gel fractions after isoelectric focusing, two distinct peaks of enzyme activity (pI1 - 5.8, pI2 = 6.4) were detected, suggesting the existence of more than one type of catalytic subunit in mouse brain cell membranes.
小鼠脑去污剂增溶制剂中Mn2+刺激的腺苷酸环化酶(ATP焦磷酸裂解酶-(环化),EC 4.6.1.1)活性。虽然NaF刺激的活性在增溶和0-4℃储存时均降低,但该酶受Mn2+刺激的能力可维持长达一周。通过在等电聚焦后的凝胶组分中腺苷酸环化酶测定中加入Mn2+,检测到两个不同的酶活性峰(pI1 - 5.8,pI2 = 6.4),这表明小鼠脑细胞膜中存在不止一种类型的催化亚基。