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Biochem J. 1988 Dec 15;256(3):989-94. doi: 10.1042/bj2560989.
2
Synthesis of lysine-containing sulphonium salts and their properties as proteinase inhibitors.含赖氨酸的锍盐的合成及其作为蛋白酶抑制剂的性质。
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引用本文的文献

1
The synthesis of inhibitors for processing proteinases and their action on the Kex2 proteinase of yeast.加工蛋白酶抑制剂的合成及其对酵母Kex2蛋白酶的作用。
Biochem J. 1993 Jul 1;293 ( Pt 1)(Pt 1):75-81. doi: 10.1042/bj2930075.

本文引用的文献

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A new method for labelling the active center of chymotrypsin.一种标记胰凝乳蛋白酶活性中心的新方法。
Biochem Biophys Res Commun. 1962 Feb 20;7:36-40. doi: 10.1016/0006-291x(62)90140-7.
2
Cathepsin B, Cathepsin H, and cathepsin L.组织蛋白酶B、组织蛋白酶H和组织蛋白酶L。
Methods Enzymol. 1981;80 Pt C:535-61. doi: 10.1016/s0076-6879(81)80043-2.
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Characterization of proinsulin- and proglucagon-converting activities in isolated islet secretory granules.分离胰岛分泌颗粒中胰岛素原和胰高血糖素原转化活性的表征
J Cell Biol. 1981 Aug;90(2):312-22. doi: 10.1083/jcb.90.2.312.
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Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases.肽基重氮甲基酮是硫醇蛋白酶的特异性失活剂。
J Biol Chem. 1981 Feb 25;256(4):1923-8.
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Inactivation of cathepsin B by active site-directed disulfide exchange. Application in covalent affinity chromatography.
J Biol Chem. 1983 Sep 10;258(17):10227-32.
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Structure of mouse kallikrein gene family suggests a role in specific processing of biologically active peptides.小鼠激肽释放酶基因家族的结构表明其在生物活性肽的特定加工过程中发挥作用。
Nature. 1983 May 26;303(5915):300-7. doi: 10.1038/303300a0.
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Plasminogen activator of islets of Langerhans: modulation by glucose and correlation with insulin production.胰岛纤溶酶原激活剂：受葡萄糖调节及其与胰岛素分泌的相关性
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8
Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor.用于加工酵母前体α因子所需的赖氨酸-精氨酸裂解内肽酶的假定结构基因的分离。
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9
Proteolysis in neuropeptide processing and other neural functions.神经肽加工及其他神经功能中的蛋白水解作用。
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10
Identification of a 31,500 molecular weight islet cell protease as cathepsin B.鉴定出一种分子量为31,500的胰岛细胞蛋白酶为组织蛋白酶B。
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具有两个阳离子残基的肽基甲基锍盐作为激素原加工潜在抑制剂的合成及性质

The synthesis and properties of peptidylmethylsulphonium salts with two cationic residues as potential inhibitors of prohormone processing.

作者信息

Zumbrunn A, Stone S, Shaw E

机构信息

Friedrich Miescher-Institut, Basel, Switzerland.

出版信息

Biochem J. 1988 Dec 15;256(3):989-94. doi: 10.1042/bj2560989.

DOI:10.1042/bj2560989
PMID:3223967
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1135513/
Abstract

Peptidylmethylsulphonium salts incorporating consecutive basic residues at the C-terminus of the peptidyl portion such as -Arg-Arg-, -Arg-Lys-, -Lys-Lys- and -Lys-Arg- were synthesized and examined as proteinase inhibitors. Serine proteinases with a specificity directed towards hydrolysis at cationic residues were found to be unaffected by these derivatives. On the other hand, cysteine proteinases, cathepsin B and, in particular, clostripain were readily inactivated by affinity labelling. The reagents thus are of promise for the study of prohormone processing promoted by cysteine proteinases.

摘要

合成了在肽基部分C末端含有连续碱性残基（如-Arg-Arg-、-Arg-Lys-、-Lys-Lys-和-Lys-Arg-）的肽基甲基磺酸盐，并将其作为蛋白酶抑制剂进行了研究。发现对阳离子残基水解具有特异性的丝氨酸蛋白酶不受这些衍生物的影响。另一方面，半胱氨酸蛋白酶、组织蛋白酶B，尤其是梭菌蛋白酶很容易通过亲和标记而失活。因此，这些试剂有望用于研究由半胱氨酸蛋白酶促进的激素原加工过程。