泌乳大鼠乳腺精氨酸酶的动力学及几种氨基酸的抑制作用。

J M Fuentes, M L Campo, G Soler
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引用次数: 20

摘要

研究了泌乳大鼠乳腺精氨酸酶的动力学和调控特性。在pH 7.4时,即在接近生理条件下,过量底物有抑制作用,Km值为9.5 mM,略低于pH 9.8时观察到的18 mM(最大酶活性)。研究了脯氨酸、鸟氨酸、赖氨酸和某些支链氨基酸对泌乳大鼠乳腺精氨酸酶活性的影响:赖氨酸、鸟氨酸和缬氨酸对泌乳大鼠乳腺精氨酸酶具有较强的竞争性抑制作用,Ki值分别为1.2 mM、1.1 mM和3.6 mM。其他氨基酸(脯氨酸、异亮氨酸和亮氨酸)也抑制泌乳大鼠乳腺精氨酸酶,但程度较轻。
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Kinetics and inhibition by some aminoacids of lactating rat mammary gland arginase.

Some kinetic and regulatory properties of lactating rat mammary gland arginase were studied. At pH 7.4, i.e. at near-physiological conditions, there was evidence of inhibition by excess of substrate, with a Km value of 9.5 mM, slightly lower than the value of 18 mM observed at pH 9.8 (maximum enzyme activity). A study was also made of the effects of proline, ornithine, lysine and certain branched-chain aminoacids on enzyme activity: lactating rat mammary gland arginase was strongly and competitively inhibited by lysine, ornithine and valine, with Ki values of 1.2 mM, 1.1 mM and 3.6 mM, respectively. Other aminoacids (proline, isoleucine and leucine) also inhibited lactating rat mammary gland arginase, although to a lesser extent.

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