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In situ kinetics of renal o-glucuronidase in teleost, Labeo rohita (Hamilton)

机译:硬骨鱼类Labeo rohita(Hamilton)中肾o-葡萄糖醛酸苷酶的原位动力学

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摘要

o-Glucuronidase is the lysosomal enzyme that increases in the tissues of animals in response to xenobiotics entering the body. Kidney is one of the organs where all the xenobiotics can be carried along with the blood for filtration, and therefore, this enzyme may be present in large amount. Ours is probably the first attempt in the teleost to study the kinetics of enzyme o-glucuronidase. It has been observed that this enzyme exhibits highest activity at pH 5 in the solution of 0.1 M acetate buffer at 38pC. Enhanced activity was noted at 52pC. However, activity starts declining up to 70pC, but above this temperature, the enzyme activity is completely inhibited, indicating heat-stable behavior. Five hours incubation at 38pC was the maximum time required to accomplish the reaction. The increase both in the substrate and in the enzyme concentration increased the reaction velocity. The Vmax and Michaelis constant (Km) recorded in the present study are 8.83 og/h and 1.33 mM. The present study will have importance in understanding the basic health of fish.
机译:o-葡糖醛酸糖苷酶是一种溶酶体酶,响应于进入人体的异生物素而在动物组织中增加。肾脏是所有异种生物都可以随血液一起过滤的器官之一,因此,这种酶可能大量存在。我们的研究可能是硬骨鱼类中首次尝试研究O-葡萄糖醛酸苷酶的动力学。已经观察到该酶在pH为5的0.1p乙酸盐缓冲液在38pC的溶液中表现出最高的活性。在52pC时发现活性增强。然而,活性开始下降至70pC,但在此温度以上,酶的活性被完全抑制,表明其具有热稳定性。在38pC下孵育5小时是完成反应所需的最长时间。底物和酶浓度的增加都增加了反应速度。本研究中记录的Vmax和米氏常数(Km)为8.83 og / h和1.33 mM。本研究将对了解鱼类的基本健康状况具有重要意义。

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