Hassan F, El-Hawary M F, El-Ghazawy A
Z Ernahrungswiss. 1981 Mar;20(1):44-54. doi: 10.1007/BF02027957.
Non-specific acid and alkaline phosphomonoesterases could be demonstrated in two viperids (Cerastes cerastes and Cerastes vipers) and two elapids (Naja haje and Naja nigricollis). The latter could be a natural source for the production of these enzymes. The activities of both enzymes in elapids were greater than in viperids. N. nigricollis was the only to show acid phosphatase activity exceeding its alkaline one. The optimum pH values recorded for acid phosphatase was 4.0 and 4.9 and for alkaline phosphatase 9.0 and 10.0 in viperids and elapids, respectively. Optimum substrate concentration for both enzymes in viperids was 0.01 M, while for acid phosphatase in N. haje and N. nigricollis it was 0.125 and 0.150 M; and for their alkaline phosphatases the values were 0.150 and 0.125 M, respectively. Mg++ behaved as an activator for both enzymes in all venoms investigated, while Zn++ showed either no or slight activating effect. Fluoride ions as well as EDTA showed certain inhibitory action. Both enzymes in the crude venoms were heat-labile.
在两种蝰蛇（角蝰和锯鳞蝰）和两种眼镜蛇（埃及眼镜蛇和黑颈眼镜蛇）中可检测到非特异性酸性和碱性磷酸单酯酶。后者可能是这些酶产生的天然来源。眼镜蛇中这两种酶的活性均高于蝰蛇。黑颈眼镜蛇是唯一酸性磷酸酶活性超过碱性磷酸酶活性的蛇类。在蝰蛇和眼镜蛇中，酸性磷酸酶记录的最佳pH值分别为4.0和4.9，碱性磷酸酶的最佳pH值分别为9.0和10.0。蝰蛇中这两种酶的最佳底物浓度均为0.01 M，而埃及眼镜蛇和黑颈眼镜蛇中酸性磷酸酶的最佳底物浓度分别为0.125 M和0.150 M；它们碱性磷酸酶的最佳底物浓度分别为0.150 M和0.125 M。在所有研究的毒液中，Mg++对这两种酶均起激活作用，而Zn++要么没有激活作用，要么只有轻微的激活作用。氟离子以及EDTA表现出一定的抑制作用。粗毒液中的这两种酶都对热不稳定。
