Is elastomucoproteinase a double-headed enzyme?

G Cs-Szabó, E Gyáni, I Banga, P Elödi
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引用次数: 0

Abstract

During isolation pancreatic elastase is accompanied by a minor component, elastomucoproteinase (EMPase), which can be separated in pure state by anion-exchange chromatography. EMPase exhibits both proteolytic and mucolytic activities. Applying powdered aortic preparations as a substrate, the enzyme can split off carbohydrate moieties, but it can also cleave peptide bonds as a proteinase. Assaying with tripeptide-p-nitroanilide substrates, the enzyme can decompose only those substrates which contain Phe or Tyr at the C-terminal. It appeared that the binding of Bz-Ala-Gly-Phe-pNA was the best, while the hydrolysis of Bz-Ala-Pro-Tyr-pNA was the fastest. Proteolytic activity of EMPase can be completely inhibited with phenylmethanesulphonyl fluoride, whereas its mucolytic activity only by 20%. The two activities may be located at two separate sites. The enzyme seemed to be composed of a single polypeptide chain by SDS-gel electrophoresis in the presence of urea and beta-mercapto-ethanol.

弹性蛋白酶是一种双头酶吗?
在分离过程中,胰腺弹性酶还含有一种小成分,即弹性蛋白酶(EMPase),该成分可通过阴离子交换色谱法在纯状态下分离。EMPase具有蛋白水解和黏液水解活性。使用粉末状主动脉制剂作为底物,该酶可以分离碳水化合物部分,但它也可以作为蛋白酶裂解肽键。对于三肽-对硝基苯胺底物,该酶只能分解c端含有苯丙氨酸或酪氨酸的底物。结果表明,Bz-Ala-Gly-Phe-pNA的结合效果最好,而Bz-Ala-Pro-Tyr-pNA的水解速度最快。苯甲磺酰氟可以完全抑制EMPase的蛋白水解活性,而其黏液水解活性仅为20%。这两项活动可以在两个不同的地点进行。在尿素和巯基乙醇的存在下,sds -凝胶电泳表明该酶由单肽链组成。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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