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人脑脊液中强啡肽转化酶的检测及生化特性分析

Assay and biochemical characterization of a dynorphin converting enzyme in human cerebrospinal fluid.

作者信息

Nyberg F, Lyrenäs S, Terenius L

机构信息

Department of Pharmacology, University of Uppsala, Sweden.

出版信息

NIDA Res Monogr. 1986;75:251-4.

PMID:2893268
Abstract

An endopeptidase hydrolyzing dynorphins A and B and alpha-neo-endorphin at the Arg6-Arg7 or Arg6-Lys7 bonds, was partially purified from human cerebrospinal fluid and further characterized by various biochemical techniques including HPLC gel permeation (UltroPac TSK G3000SW) and ion exchange (TSK DEAE-3SW) chromatography. A procedure for quantitative analysis of the enzyme in individual CSF samples is also described. The activity in lumbar CSF of women in late pregnancy was significantly lower than that in control samples.

摘要

一种内肽酶可在精氨酸6 - 精氨酸7或精氨酸6 - 赖氨酸7键处水解强啡肽A、B和α-新内啡肽,该酶从人脑脊液中部分纯化,并通过包括高效液相色谱凝胶渗透(UltroPac TSK G3000SW)和离子交换(TSK DEAE - 3SW)色谱在内的各种生化技术进一步表征。还描述了一种对个体脑脊液样本中该酶进行定量分析的方法。妊娠晚期女性腰段脑脊液中的活性明显低于对照样本。

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引用本文的文献

1
Metabolism of dynorphin A1-13 in human CSF.强啡肽A1-13在人脑脊液中的代谢
Neurochem Res. 1996 Oct;21(10):1213-9. doi: 10.1007/BF02532398.