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通过鸟氨酸脱羧酶反应的终产物诱导产生一种蛋白质抑制剂。

Induction of a protein inhibitor to ornithine decarboxylase by the end products of its reaction.

作者信息

Heller J S, Fong W F, Canellakis E S

出版信息

Proc Natl Acad Sci U S A. 1976 Jun;73(6):1858-62. doi: 10.1073/pnas.73.6.1858.

DOI:10.1073/pnas.73.6.1858
PMID:1064859
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC430406/
Abstract

Putrescine, the end-product of ornithine decarboxylase (ODC: L-ornithine carboxylyase, EC; 4.1.1.17) action, induces the synthesis of a protein(s), in L1210, neuroblastoma, and H-35 cells as well as in rat liver, which inhibits ODC activity. Spermidine and spermine, distal products of ODC activity, also induce the synthesis of a similar protein in H-35 cells. These ODC-inhibitors are heat-labile, trypsin-sensitive, and their induction is dependent upon protein synthesis. They have short half-lives which range from 18 to 66 min; these half-lives are similar to those of the ODC derived from the same source. They are noncompetitive inhibitors of ODC activity with an apparent molecular weight of 26,500. Each inhibitor crossreacts with the ODC's of the other cells and forms an enzyme-inhibitor complex which is stable during Sephadex chromatography; however, after treatment with ammonium sulfate, enzyme and inhibitor activities can be dissociated and recovered intact from the same column. We propose the name antizyme for proteins whose synthesis is induced by the proximal or distal products of the enzyme they inhibit.

摘要

腐胺是鸟氨酸脱羧酶(ODC:L-鸟氨酸羧化酶,EC;4.1.1.17)作用的终产物,它能在L1210细胞、神经母细胞瘤细胞、H-35细胞以及大鼠肝脏中诱导一种蛋白质的合成,该蛋白质可抑制ODC活性。亚精胺和精胺是ODC活性的下游产物,它们也能在H-35细胞中诱导合成一种类似的蛋白质。这些ODC抑制剂对热不稳定,对胰蛋白酶敏感,其诱导作用依赖于蛋白质合成。它们的半衰期较短,在18至66分钟之间;这些半衰期与来自同一来源的ODC的半衰期相似。它们是ODC活性的非竞争性抑制剂,表观分子量为26,500。每种抑制剂都能与其他细胞的ODC发生交叉反应,并形成一种酶-抑制剂复合物,该复合物在葡聚糖凝胶层析过程中是稳定的;然而,用硫酸铵处理后,酶和抑制剂的活性可以解离,并从同一柱上完整回收。我们建议将由它们所抑制的酶的近端或远端产物诱导合成的蛋白质命名为抗酶。

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Induction of a protein inhibitor to ornithine decarboxylase by the end products of its reaction.通过鸟氨酸脱羧酶反应的终产物诱导产生一种蛋白质抑制剂。
Proc Natl Acad Sci U S A. 1976 Jun;73(6):1858-62. doi: 10.1073/pnas.73.6.1858.
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