Dolgikh M S, Blagoveshchenskiĭ V A
Vopr Med Khim. 1975 Mar-Apr;21(2):143-7.
Five strains of A type Cl. perfringens of different titres of toxicity (BP6K, SR-12, 2836, 2910, 1) possessed a distinct activity of ornithine transcarbamylase. In cells the maximal activity of the enzyme was observed within 3-5 hrs of growth of the culture. The enzyme was partially purified and some of its physico-chemical properties were studied. Ornithine transcarbamylase was termostable. Monoiodine acetate, p-chloromercurybenzoate, semicarbazide, Hg-2+, Cu-2+ and Fe-3+ inhibited the enzymatic activity, but Mg-2+ and Ca-2+ activated the enzyme. Ornithine transcarbamylase was shown to be active in wide region of pH: from pH 6.0 to pH 9.0 and higher. Two peaks of the enzyme activity were observed: the first (a more distinct one) at pH 8.6-8.9 and the second, smaller,--at pH 6.5-6.7.
五株不同毒性效价的A型产气荚膜梭菌（BP6K、SR - 12、2836、2910、1）具有明显的鸟氨酸转氨甲酰酶活性。在细胞中，培养物生长3 - 5小时内观察到该酶的最大活性。该酶经过部分纯化，并对其一些理化性质进行了研究。鸟氨酸转氨甲酰酶具有热稳定性。碘乙酸、对氯汞苯甲酸、氨基脲、Hg²⁺、Cu²⁺和Fe³⁺抑制酶活性，但Mg²⁺和Ca²⁺激活该酶。鸟氨酸转氨甲酰酶在较宽的pH范围内具有活性：从pH 6.0至pH 9.0及更高。观察到酶活性有两个峰值：第一个（更明显）在pH 8.6 - 8.9，第二个较小，在pH 6.5 - 6.7。
