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两种需要锰来激活的小鼠肝脏碱性磷酸酶的部分特性分析。

Partial characterization of two mouse liver alkaline phosphatases that require manganese for activity.

作者信息

Kinnett D G, Wilcox F H

出版信息

Int J Biochem. 1982;14(11):977-81. doi: 10.1016/0020-711x(82)90058-1.

DOI:10.1016/0020-711x(82)90058-1
PMID:7141074
Abstract

Two manganese requiring isozymes of alkaline phosphatase from the liver of the house mouse (Mus musculus)were studied to determine their properties and location within the cell. 2. The two isozymes, referred to as Region I and Region III, were located in the cytosol from liver homogenates. 3. Optimum activity for Region I isozyme at 37 degrees C was obtained at pH 9.1 and a manganese concentration of 0.5 mM. 4. Optimum conditions for Region III isozyme were pH 7.4 and 5.0 mM manganese. 5. Both isozymes were stable at 56 degrees C; Region III isozyme was stable at 65 degrees C, but Region I isozyme was partially deactivated to 35% of its original activity. 6. Both isozymes were completely deactivated at 75 degrees C within 30 min. Region I isozyme was inhibited by 10 mM L-homoarginine (30% of original activity) and 2.5 mM L-phenylalanine (66% of original activity). 7. No inhibition occurred with Region III isozyme in the presence of either chemical.

摘要

对家鼠(小家鼠)肝脏中两种需要锰的碱性磷酸酶同工酶进行了研究,以确定它们的性质和在细胞内的位置。2. 这两种同工酶,分别称为区域I和区域III,位于肝脏匀浆的胞质溶胶中。3. 区域I同工酶在37摄氏度时的最佳活性在pH 9.1和锰浓度为0.5 mM时获得。4. 区域III同工酶的最佳条件是pH 7.4和5.0 mM锰。5. 两种同工酶在56摄氏度时都很稳定;区域III同工酶在65摄氏度时稳定,但区域I同工酶部分失活至其原始活性的35%。6. 两种同工酶在75摄氏度下30分钟内完全失活。区域I同工酶被10 mM L-高精氨酸(原始活性的30%)和2.5 mM L-苯丙氨酸(原始活性的66%)抑制。7. 在存在任何一种化学物质的情况下,区域III同工酶均未受到抑制。

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