贻贝紫贻贝外套膜中天冬氨酸转氨甲酰酶的部分特性分析

Partial characterisation of aspartate transcarbamylase from the mantle of the mussel Mytilus edulis.

作者信息

Mathieu M

出版信息

Comp Biochem Physiol B. 1985;82(4):667-74. doi: 10.1016/0305-0491(85)90505-x.

Abstract

The stability and the effect of pH and temperature on the activity of aspartate transcarbamylase from mantle of mussel were studied. The Km values for aspartic acid and carbamylphosphate at 35 degrees C are 1.8 X 10(-2) M and 7 X 10(-3) M respectively, values of Vmax being identical at 17.54 nM carbamylaspartate formed/min/mg protein. Allosteric effectors of ATCase (ATP and CTP) have no effect on the activity of mantle ATCase. PHMB and Cu2+ are strong inhibitors of the ATCase activity, organic solvents (DMF, DMSO) having a strong stimulatory action. ATCase from mantle of mussel has been compared to ATCase from different sources.

摘要

研究了贻贝外套膜中天冬氨酸转氨甲酰酶的稳定性以及pH和温度对其活性的影响。在35℃时，天冬氨酸和氨甲酰磷酸的Km值分别为1.8×10⁻²M和7×10⁻³M，Vmax值相同，为每分钟每毫克蛋白质形成17.54 nM氨甲酰天冬氨酸。天冬氨酸转氨甲酰酶（ATCase）的别构效应剂（ATP和CTP）对外套膜ATCase的活性没有影响。聚六亚甲基双胍（PHMB）和Cu²⁺是ATCase活性的强抑制剂，有机溶剂（DMF、DMSO）具有强烈的刺激作用。已将贻贝外套膜中的ATCase与来自不同来源的ATCase进行了比较。