Effect of Mn2+ on Glutathione-S-Transferase Activity of Human Ejaculated Spermatozoa

Kuldeep Kaushik, P. K. Mittal, N. Kalla
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引用次数: 1

Abstract

This study was undertaken to monitor the effect of 0.1 mM Mn2+ on the glutathione s-transferase activity (GST) in nicotine treated and untreated spermatozoa samples and to calculate the Michalis-Menten kinetic parameter of the reaction. Semen samples were collected from healthy volunteer donors after semen analysis, sample was subjected for preparation of 10,000 g supernatant. The enzymatic activity has been performed using 1-chloro, 2-4 dinitrobenzene (CDNB) as a substrate. The 0.1 mM Mn2+ supplementation was found to decrease the GST activities significantly (p<0.001). CDNB-GSH conjugate formation were almost significantly (p<0.05) lowered down with the addition of 0.1 mM Mn2+ to nicotine treated samples. The substrate affinity constant (km) of the reaction was found to be 44.44 μM. It remained unchanged throughout the Vmax which was considerably lowered upon Mn2+ addition to the spermatozoal samples. The data was transformed to Lineweaver-Burk 1/v vs 1/[S] plot which indicate the behavior of this enzyme was non-competitive in nature.
Mn2+对人射精精子谷胱甘肽- s转移酶活性的影响
本研究监测0.1 mM Mn2+对尼古丁处理和未处理的精子谷胱甘肽s-转移酶活性(GST)的影响,并计算反应的Michalis-Menten动力学参数。采集健康志愿者精液分析后的精液样本,制备10000 g上清液。以1-氯,2-4二硝基苯(CDNB)为底物进行酶活性研究。添加0.1 mM Mn2+显著降低GST活性(p<0.001)。烟碱处理样品中添加0.1 mM Mn2+后,CDNB-GSH缀合物的形成几乎显著降低(p<0.05)。该反应的底物亲和常数(km)为44.44 μM。它在整个Vmax中保持不变,在精子样品中添加Mn2+后,Vmax大大降低。数据转化为Lineweaver-Burk 1/v vs 1/[S]图,表明该酶的行为本质上是非竞争性的。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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