Purification and crystallization of the extracellular domain of human neutral endopeptidase (neprilysin) expressed in Pichia pastoris

Glenn E. Dale; Brigitte DArcy; Chantana YuvaniyamaBeat WipfChristian OefnerAllan DArcy

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Purification and crystallization of the extracellular domain of human neutral endopeptidase (neprilysin) expressed in Pichia pastoris

机译：净化和结晶人类中性细胞外的领域肽链内切酶在毕赤酵母属(neprilysin)表示

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Neutral endopeptidase (NEP) is a mammalian zinc metalloprotease involved in the inactivation of a wide variety of regulatory peptides such as enkephalins and atrial natiuretic factor. The soluble extracellular domain of NEP (sNEP) was expressed in the methylotrophic yeast Pichia pastoris. The protein was purified to homogeneity and single crystals have been obtained. Enzymatic deglycosylation of the enzyme was essential for the production of crystals suitable for X-ray analysis for both the NEP-phosphoramidon binary complex and the apo enzyme.

机译：中性肽链内切是一种哺乳动物的锌metalloprotease参与的失活各种各样的监管肽等肽和心房有natiuretic因素。可溶性细胞外棉结(sNEP)的领域表示在methylotrophic毕赤酵母属酵母pastoris。和单晶。deglycosylation酶是必不可少的生产适合x射线晶体分析NEP-phosphoramidon二进制复杂和朊酶。

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《Acta crystallographica.Section D. Biological crystallography》 |2000年第7期|894-897|共4页
作者
Glenn E. Dale; Brigitte DArcy; Chantana YuvaniyamaBeat WipfChristian OefnerAllan DArcy;
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F. Hoffmann-La Roche Ltd Pharma Preclinical Research, CH-4070, Basel, Switzerland;

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正文语种英语
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关键词
single crystals; Neprilysin; EnkephalinshomogeneityX-ray analysisPurificationKomagataella pastorisEnzymesExtracellular DomainCrystallization;

机译：单pastorisEnzymesExtracellularDomainCrystallization;

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Purification and crystallization of the extracellular domain of human neutral endopeptidase (neprilysin) expressed in Pichia pastoris

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