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人组织中黄嘌呤氧化还原酶活性的分布——一项组织化学与生物化学研究

Distribution of xanthine oxidoreductase activity in human tissues--a histochemical and biochemical study.

作者信息

Kooij A, Schijns M, Frederiks W M, Van Noorden C J, James J

机构信息

Laboratory of Cell Biology and Histology, University of Amsterdam, The Netherlands.

出版信息

Virchows Arch B Cell Pathol Incl Mol Pathol. 1992;63(1):17-23. doi: 10.1007/BF02899240.

DOI:10.1007/BF02899240
PMID:1362018
Abstract

Localization of the activity of both the dehydrogenase and oxidase forms of xanthine oxidoreductase were studied in biopsy and postmortem specimens of various human tissues with a recently developed histochemical method using unfixed cryostat sections, poly-(vinyl alcohol) as tissue stabilizator, 1-methoxyphenazine methosulphate as intermediate electron acceptor and Tetranitro BT as final electron acceptor. High enzyme activity was found only in the liver and jejunum, whereas all the other organs studied showed no activity. In the liver, enzyme activity was found in sinusoidal cells and both in periportal and pericentral hepatocytes. In the jejunum, enterocytes and goblet cells, as well as the lamina propria beneath the basement membrane showed activity. The oxidase activity and total dehydrogenase and oxidase activity of xanthine oxidoreductase, as determined biochemically, were found in the liver and jejunum, but not in the kidney and spleen. This confirmed the histochemical results for these organs. Autolytic rat livers several hours after death were studied to exclude artefacts due to postmortem changes in the human material. These showed loss of activity both histochemically and biochemically. However, the percentage activity of xanthine oxidase did not change significantly in these livers compared with controls. The findings are discussed with respect to the possible function of the enzyme. Furthermore, the low conversion rate of xanthine dehydrogenase into xanthine oxidase during autolysis is discussed in relation to ischemia-reperfusion injury.

摘要

采用一种最新研发的组织化学方法,以未固定的低温恒温切片、聚(乙烯醇)作为组织稳定剂、1-甲氧基吩嗪硫酸甲酯作为中间电子受体以及四硝基蓝四唑作为最终电子受体,对各种人体组织的活检和尸检标本中黄嘌呤氧化还原酶的脱氢酶和氧化酶形式的活性定位进行了研究。仅在肝脏和空肠中发现了高酶活性,而所研究的所有其他器官均未显示活性。在肝脏中,酶活性存在于窦状细胞以及门周和中央周围的肝细胞中。在空肠中,肠上皮细胞、杯状细胞以及基底膜下方的固有层显示出活性。通过生化方法测定,黄嘌呤氧化还原酶的氧化酶活性以及总脱氢酶和氧化酶活性在肝脏和空肠中存在,但在肾脏和脾脏中不存在。这证实了这些器官的组织化学结果。对死后数小时的自溶大鼠肝脏进行了研究,以排除人体材料中死后变化导致的假象。这些肝脏在组织化学和生化方面均显示出活性丧失。然而,与对照相比,这些肝脏中黄嘌呤氧化酶的活性百分比没有显著变化。针对该酶的可能功能对研究结果进行了讨论。此外,还讨论了自溶过程中黄嘌呤脱氢酶向黄嘌呤氧化酶的低转化率与缺血再灌注损伤的关系。

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Distribution of xanthine oxidoreductase activity in human tissues--a histochemical and biochemical study.人组织中黄嘌呤氧化还原酶活性的分布——一项组织化学与生物化学研究
Virchows Arch B Cell Pathol Incl Mol Pathol. 1992;63(1):17-23. doi: 10.1007/BF02899240.
2
The proportion of xanthine oxidase activity of total xanthine oxidoreductase activity in situ remains constant in rat liver under various (patho)physiological conditions.在各种(病理)生理条件下,大鼠肝脏中黄嘌呤氧化酶活性占总黄嘌呤氧化还原酶活性的比例保持恒定。
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Localization of xanthine oxidoreductase activity using the tissue protectant polyvinyl alcohol and final electron acceptor Tetranitro BT.使用组织保护剂聚乙烯醇和最终电子受体四硝基BT对黄嘌呤氧化还原酶活性进行定位
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A quantitative histochemical procedure for the demonstration of purine nucleoside phosphorylase activity in rat and human liver using Tetranitro BT and xanthine oxidase as auxiliary enzyme.一种使用四硝基BT和黄嘌呤氧化酶作为辅助酶来显示大鼠和人肝脏中嘌呤核苷磷酸化酶活性的定量组织化学方法。
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Conversion of xanthine dehydrogenase into xanthine oxidase in rat liver and plasma at the onset of reperfusion after ischemia.缺血后再灌注开始时大鼠肝脏和血浆中黄嘌呤脱氢酶向黄嘌呤氧化酶的转化。
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The effect of ischaemia on xanthine oxidase activity in rat intestine and liver.缺血对大鼠肠道及肝脏中黄嘌呤氧化酶活性的影响。
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A quantitative histochemical study of xanthine oxidase activity in rat liver using the cerium capture method in the presence of polyvinyl alcohol.在聚乙烯醇存在的情况下,使用铈捕获法对大鼠肝脏中的黄嘌呤氧化酶活性进行定量组织化学研究。
J Histochem Cytochem. 1994 Aug;42(8):1091-6. doi: 10.1177/42.8.8027528.
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A histochemical procedure for light microscopic demonstration of xanthine oxidase activity in unfixed cryostat sections using cerium ions and a semipermeable membrane technique.一种利用铈离子和半透膜技术在未固定的低温恒温器切片中进行光镜下黄嘌呤氧化酶活性组织化学显示的方法。
J Histochem Cytochem. 1993 May;41(5):667-70. doi: 10.1177/41.5.8468447.

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Aldehyde oxidase functions as a superoxide generating NADH oxidase: an important redox regulated pathway of cellular oxygen radical formation.醛氧化酶作为一种超氧化物生成 NADH 氧化酶发挥作用:这是细胞氧自由基形成的一个重要氧化还原调节途径。
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Role of xanthine oxidoreductase as an antimicrobial agent.黄嘌呤氧化还原酶作为一种抗菌剂的作用。
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