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阿司匹林酶与需要巯基的一种羧酸酯酶的鉴定。

Identification of aspirinase with one of the carboxylesterases requiring a thiol group.

作者信息

White K N, Hope D B

出版信息

Biochem J. 1981 Sep 1;197(3):771-3. doi: 10.1042/bj1970771.

DOI:10.1042/bj1970771
PMID:7325988
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1163196/
Abstract

Aspirin-hydrolysing activity in guinea-pig liver is located mainly in the microsomal fraction. This activity was found by electrophoresis to be due to a single carboxylesterase band, out of 12 bands revealed with alpha-naphthyl acetate as substrate. The activity is inhibited completely and irreversibly by the carboxylesterase inhibitor bis-(-4-nitrophenyl) hydrogen phosphate, and also by thiol-blocking reagents.

摘要

豚鼠肝脏中的阿司匹林水解活性主要位于微粒体部分。通过电泳发现，以乙酸α-萘酯为底物显示的12条带中，这种活性归因于单一的羧酸酯酶带。该活性被羧酸酯酶抑制剂双（-4-硝基苯基）磷酸氢完全不可逆地抑制，也被硫醇阻断剂抑制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fd30/1163196/8020f4b87a29/biochemj00394-0241-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fd30/1163196/8020f4b87a29/biochemj00394-0241-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fd30/1163196/8020f4b87a29/biochemj00394-0241-a.jpg

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本文引用的文献

1
DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS.圆盘电泳。II. 方法及其在人血清蛋白中的应用。
Ann N Y Acad Sci. 1964 Dec 28;121:404-27. doi: 10.1111/j.1749-6632.1964.tb14213.x.
2
A new and rapid colorimetric determination of acetylcholinesterase activity.一种新的快速比色法测定乙酰胆碱酯酶活性。
Biochem Pharmacol. 1961 Jul;7:88-95. doi: 10.1016/0006-2952(61)90145-9.
3
Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue.组织分级分离研究。6. 大鼠肝脏组织中酶的细胞内分布模式。
人体内酯酶的临床意义。
Clin Pharmacokinet. 1985 Sep-Oct;10(5):392-403. doi: 10.2165/00003088-198510050-00002.
Biochem J. 1955 Aug;60(4):604-17. doi: 10.1042/bj0600604.
4
A simple procedure for the isolation of rat liver microsomes.
FEBS Lett. 1971 Sep 15;17(1):90-92. doi: 10.1016/0014-5793(71)80571-9.
5
Selective inhibition of rat liver carboxylesterases by various organophosphorus diesters in vivo and in vitro.多种有机磷二酯在体内和体外对大鼠肝脏羧酸酯酶的选择性抑制作用。
Biochem Pharmacol. 1980 Jul 1;29(13):1927-31. doi: 10.1016/0006-2952(80)90105-7.
6
A simultaneous-coupling azo dye method for the quantitative assay of esterase using alpha-naphthyl acetate as substrate.一种以醋酸α-萘酯为底物的酯酶定量测定的偶联偶氮染料同步法。
Histochem J. 1980 Mar;12(2):221-34. doi: 10.1007/BF01024552.
7
Influence of the route of administration on the area under the plasma concentration-time curve.给药途径对血浆浓度-时间曲线下面积的影响。
J Pharm Sci. 1969 Jan;58(1):71-5. doi: 10.1002/jps.2600580114.
8
[Phosphoric acid-bis-(p-nitro-phenylester), a new inhibitor of microsomal carboxylesterases].磷酸 - 双 -（对硝基 - 苯酯），一种新型微粒体羧酸酯酶抑制剂
Hoppe Seylers Z Physiol Chem. 1967 Jun;348(6):609-19.
9
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Eur J Biochem. 1971 Nov 11;23(2):303-13. doi: 10.1111/j.1432-1033.1971.tb01622.x.
10
Characterization of the esterases of guinea pig liver and kidney.
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