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大鼠肺和肝微粒体细胞色素P-450酶活性对储存的稳定性:纯化的微粒体组分、线粒体后组分和全组织。

Stability of rat lung and liver microsomal cytochrome P-450 enzyme activities to storage: purified microsomal fraction, postmitochondrial fraction, and whole tissue.

作者信息

Danner-Rabovsky J, Groseclose R D

出版信息

J Toxicol Environ Health. 1982 Oct-Nov;10(4-5):601-11. doi: 10.1080/15287398209530279.

DOI:10.1080/15287398209530279
PMID:7161816
Abstract

The ability to maintain cytochrome P-450 enzyme levels in stored tissue samples is necessary in order to properly utilize this enzyme system in toxicological and environmental health studies. The stability of enzyme activities associated with microsomal cytochrome P-450 was investigated to determine the best way to handle large numbers of samples and postmortem or biopsy lung and liver tissue. Long-term storage in cold buffer resulted in diminished activities in purified microsomes and whole tissue. Benzo[a]pyrene hydroxylase and 7-ethoxycoumarin deethylase, however, were stable when the purified microsomal fraction, postmitochondrial fraction, or whole tissue was stored at -80 degrees C, but care should be exercised in the freezing and thawing procedures.

摘要

为了在毒理学和环境卫生研究中恰当地利用细胞色素P - 450酶系统,保持储存组织样本中该酶水平的能力是必要的。研究了与微粒体细胞色素P - 450相关的酶活性稳定性,以确定处理大量样本以及死后或活检肺和肝组织的最佳方法。在冷缓冲液中长期储存会导致纯化微粒体和全组织中的活性降低。然而,当纯化的微粒体部分、线粒体后部分或全组织储存在-80摄氏度时,苯并[a]芘羟化酶和7 - 乙氧基香豆素脱乙基酶是稳定的,但在冷冻和解冻过程中应小心操作。

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Stability of rat lung and liver microsomal cytochrome P-450 enzyme activities to storage: purified microsomal fraction, postmitochondrial fraction, and whole tissue.大鼠肺和肝微粒体细胞色素P-450酶活性对储存的稳定性:纯化的微粒体组分、线粒体后组分和全组织。
J Toxicol Environ Health. 1982 Oct-Nov;10(4-5):601-11. doi: 10.1080/15287398209530279.
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引用本文的文献

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Interlaboratory comparison of total cytochrome P-450 and protein determinations in rat liver microsomes. Reinvestigation of assay conditions.大鼠肝微粒体中总细胞色素P-450和蛋白质测定的实验室间比较。分析条件的重新研究。
Arch Toxicol. 1987;61(1):27-33. doi: 10.1007/BF00324544.
2
The in vitro effects of alkanes, alcohols, and ketones on rat lung cytochrome P450-dependent alkoxyphenoxazone dealkylase activities.
Arch Toxicol. 1989;63(1):13-7. doi: 10.1007/BF00334627.