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1
Formation of native insulin from the scrambled molecule by protein disulphide-isomerase.蛋白质二硫键异构酶将无序分子转化为天然胰岛素。
Biochem J. 1988 Oct 15;255(2):451-5. doi: 10.1042/bj2550451.
2
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Protein disulphide-isomerase and the formation of native disulphide bonds.蛋白质二硫键异构酶与天然二硫键的形成
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Isomeric Replacement of a Single Aspartic Acid Induces a Marked Change in Protein Function: The Example of Ribonuclease A.单个天冬氨酸的异构体替代会引起蛋白质功能的显著变化:以核糖核酸酶A为例。
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Human αB-crystallin as fusion protein and molecular chaperone increases the expression and folding efficiency of recombinant insulin.人αB-晶体蛋白作为融合蛋白和分子伴侣可提高重组胰岛素的表达和折叠效率。
PLoS One. 2018 Oct 19;13(10):e0206169. doi: 10.1371/journal.pone.0206169. eCollection 2018.
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Action of protein disulfide isomerase on proinsulin exit from endoplasmic reticulum of pancreatic β-cells.蛋白二硫键异构酶对胰腺β细胞内质网中前胰岛素分泌的作用。
J Biol Chem. 2012 Jan 2;287(1):43-47. doi: 10.1074/jbc.C111.279927. Epub 2011 Nov 21.
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Evaluating the intrinsic cysteine redox-dependent states of the A-chain of human insulin using NMR spectroscopy, quantum chemical calculations, and mass spectrometry.使用 NMR 光谱学、量子化学计算和质谱法评估人胰岛素 A 链中半胱氨酸的氧化还原依赖态。
J Phys Chem B. 2010 Jan 14;114(1):585-91. doi: 10.1021/jp908729h.
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Intra-A chain disulphide bond forms first during insulin precursor folding.胰岛素前体折叠过程中,A链内二硫键首先形成。
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Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.还原变性的酸性磷脂酶A2的再活化需要蛋白质二硫键异构酶的异构酶活性和伴侣活性。
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8
Purification and characterization of protein disulphide-isomerase from the unicellular green alga Chlamydomonas reinhardii. A 120 kDa dimer antigenically distinct from the vertebrate enzyme.莱茵衣藻单细胞绿藻中蛋白质二硫键异构酶的纯化与特性分析。一种120 kDa的二聚体,在抗原性上与脊椎动物的酶不同。
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9
The insulin A and B chains contain structural information for the formation of the native molecule. Studies with protein disulphide-isomerase.胰岛素A链和B链包含形成天然分子的结构信息。蛋白质二硫键异构酶的研究。
Biochem J. 1990 Jun 1;268(2):429-35. doi: 10.1042/bj2680429.

本文引用的文献

1
Resynthesis of insulin from its glycyl and phenylalanyl chains.从胰岛素的甘氨酰链和苯丙氨酰链重新合成胰岛素。
Sci Sin. 1961 May;10:84-104.
2
Role of disulfide interchange enzyme in immunoglobulin synthesis.二硫键交换酶在免疫球蛋白合成中的作用。
Biochemistry. 1981 Nov 10;20(23):6594-9. doi: 10.1021/bi00526a012.
3
Protein disulphide-isomerase and the formation of native disulphide bonds.蛋白质二硫键异构酶与天然二硫键的形成
Biochem Soc Trans. 1984 Dec;12(6):929-32. doi: 10.1042/bst0120929.
4
Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase.蛋白质中二硫键的形成与异构化:蛋白质二硫键异构酶
Methods Enzymol. 1984;107:281-94. doi: 10.1016/0076-6879(84)07018-x.
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A radioreceptor assay method for insulin.一种胰岛素的放射受体测定方法。
J Biol Stand. 1984 Oct;12(4):427-34. doi: 10.1016/s0092-1157(84)80066-9.
6
Studies on the synthesis of insulin from natural and synthetic A and B chains. II. Isolation of insulin from recombination mixtures of natural A and B chains.天然及合成A链和B链合成胰岛素的研究。II. 从天然A链和B链的重组混合物中分离胰岛素。
Biochemistry. 1967 Sep;6(9):2642-54. doi: 10.1021/bi00861a002.
7
[Resynthesis of insulin from the preoxidized A chain and reduced B chain].[由预氧化的A链和还原的B链重新合成胰岛素]
Justus Liebigs Ann Chem. 1966 Feb;691:225-31. doi: 10.1002/jlac.19666910132.
8
Enzymatic destruction of immunoreactivity in proinsulin and insulin and activation of their scrambled forms.胰岛素原和胰岛素免疫反应性的酶促破坏及其无序形式的激活。
Arch Biochem Biophys. 1970 Dec;141(2):533-7. doi: 10.1016/0003-9861(70)90171-2.
9
A simple free fat cell bioassay for insulin.一种用于胰岛素的简单游离脂肪细胞生物测定法。
Horm Metab Res. 1974 Jan;6(1):12-6. doi: 10.1055/s-0028-1093895.
10
The effect of a non-peptide interchain crosslink on the reoxidation of reduced insulin.一种非肽链间交联对还原胰岛素再氧化的影响。
Hoppe Seylers Z Physiol Chem. 1973 Jun;354(6):613-27. doi: 10.1515/bchm2.1973.354.1.613.

蛋白质二硫键异构酶将无序分子转化为天然胰岛素。

Formation of native insulin from the scrambled molecule by protein disulphide-isomerase.

作者信息

Tang J G, Wang C C, Tsou C L

机构信息

Institute of Biophysics, Academia Sinica, Beijing, China.

出版信息

Biochem J. 1988 Oct 15;255(2):451-5. doi: 10.1042/bj2550451.

DOI:10.1042/bj2550451
PMID:3060111
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1135249/
Abstract

The formation of native insulin either from scrambled insulin or from the separated A chain and B chain S-sulphonates by protein disulphide-isomerase was demonstrated with yields of 20-30% as measured by h.p.l.c. analysis, receptor binding and stimulation of lipogenesis. The h.p.l.c. profile of the reaction products shows that, among all the possible isomers containing both chains, the native hormone is by far the predominating product and consequently the most stable under certain conditions.

摘要

通过蛋白质二硫键异构酶从混乱的胰岛素或从分离的A链和B链S-磺酸盐形成天然胰岛素得到了证实,通过高效液相色谱分析、受体结合和脂肪生成刺激测定,产率为20%-30%。反应产物的高效液相色谱图谱表明,在所有包含两条链的可能异构体中,天然激素是迄今为止占主导的产物,因此在某些条件下是最稳定的。