{"title":"白菖蒲可溶性氨基肽酶系统。一种新的谷氨酸氨基肽酶的表征","authors":"Pedro Fernández Murray, Susana Passeron","doi":"10.1006/emyc.1995.1026","DOIUrl":null,"url":null,"abstract":"<div><p>Fernández, Murray, P., and Passeron, S. 1995. The soluble aminopeptidase system from <em>Saccobolus platensis</em>. Characterization of a new glutamate aminopeptidase. <em>Experimental Mycology</em> 19, 214-222. The aminopeptidase pattern from the fungus <em>Saccobolus platensis</em> was investigated by ion-exchange chromatography fractionation of the soluble proteins. The chromogenic <em>p</em>-nitroanilide derivatives of nine different amino acids were used as substrates. Apart from the previously characterized major alanine aminopeptidase (P. Fernádez Murray, A. Samela, and S. Passeron, 1992. <em>Exp. Mycol.</em> 16, 279-290), two new minor aminopeptidase activities were found: one mainly a proline aminopeptidase and a second highly specific for the hydrolysis of the chromogenic derivative of glutamate. This last activity was subjected to ammonium sulfate fractionation and successive phenyl-Sepharose, DEAE-Sephacel, and Sephacryl S-200 HR column chromatography. A highly purified enzyme fraction was obtained. This new glutamate aminopeptidase had a molecular weight of 22 kDa and an optimum pH range of 7.2-8.0 and was inhibited by <em>o</em>-phenanthroline and bestatin.</p></div>","PeriodicalId":12110,"journal":{"name":"Experimental Mycology","volume":"19 3","pages":"Pages 214-222"},"PeriodicalIF":0.0000,"publicationDate":"1995-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/emyc.1995.1026","citationCount":"0","resultStr":"{\"title\":\"The Soluble Aminopeptidase System from Saccobolus platensis. Characterization of a New Glutamate Aminopeptidase\",\"authors\":\"Pedro Fernández Murray, Susana Passeron\",\"doi\":\"10.1006/emyc.1995.1026\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Fernández, Murray, P., and Passeron, S. 1995. The soluble aminopeptidase system from <em>Saccobolus platensis</em>. Characterization of a new glutamate aminopeptidase. <em>Experimental Mycology</em> 19, 214-222. The aminopeptidase pattern from the fungus <em>Saccobolus platensis</em> was investigated by ion-exchange chromatography fractionation of the soluble proteins. The chromogenic <em>p</em>-nitroanilide derivatives of nine different amino acids were used as substrates. Apart from the previously characterized major alanine aminopeptidase (P. Fernádez Murray, A. Samela, and S. Passeron, 1992. <em>Exp. Mycol.</em> 16, 279-290), two new minor aminopeptidase activities were found: one mainly a proline aminopeptidase and a second highly specific for the hydrolysis of the chromogenic derivative of glutamate. This last activity was subjected to ammonium sulfate fractionation and successive phenyl-Sepharose, DEAE-Sephacel, and Sephacryl S-200 HR column chromatography. A highly purified enzyme fraction was obtained. This new glutamate aminopeptidase had a molecular weight of 22 kDa and an optimum pH range of 7.2-8.0 and was inhibited by <em>o</em>-phenanthroline and bestatin.</p></div>\",\"PeriodicalId\":12110,\"journal\":{\"name\":\"Experimental Mycology\",\"volume\":\"19 3\",\"pages\":\"Pages 214-222\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1995-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1006/emyc.1995.1026\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Experimental Mycology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0147597585710262\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Experimental Mycology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0147597585710262","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
摘要
Fernández, Murray, P.， and Passeron, S. 1995。白菖蒲可溶性氨基肽酶系统。一种新的谷氨酸氨基肽酶的表征。真菌学通报，2009,44 - 44。采用离子交换色谱法分离可溶性蛋白，研究了真菌Saccobolus platensis的氨基肽酶谱。以9种不同氨基酸的显色对硝基苯胺衍生物为底物。除了先前描述的主要丙氨酸氨基肽酶(P. Fernádez Murray, A. Samela, and S. Passeron, 1992)。在此基础上，发现了两种新的氨基肽酶活性:一种主要是脯氨酸氨基肽酶，另一种对谷氨酸的显色衍生物的水解具有高度特异性。最后一种活性经过硫酸铵分馏和连续的苯基- sepharose、DEAE-Sephacel和Sephacryl S-200 HR柱层析。得到了高纯度的酶组分。该谷氨酸氨基肽酶分子量为22 kDa，最适pH范围为7.2 ~ 8.0，邻菲罗啉和百司他汀对其有抑制作用。
The Soluble Aminopeptidase System from Saccobolus platensis. Characterization of a New Glutamate Aminopeptidase
Fernández, Murray, P., and Passeron, S. 1995. The soluble aminopeptidase system from Saccobolus platensis. Characterization of a new glutamate aminopeptidase. Experimental Mycology 19, 214-222. The aminopeptidase pattern from the fungus Saccobolus platensis was investigated by ion-exchange chromatography fractionation of the soluble proteins. The chromogenic p-nitroanilide derivatives of nine different amino acids were used as substrates. Apart from the previously characterized major alanine aminopeptidase (P. Fernádez Murray, A. Samela, and S. Passeron, 1992. Exp. Mycol. 16, 279-290), two new minor aminopeptidase activities were found: one mainly a proline aminopeptidase and a second highly specific for the hydrolysis of the chromogenic derivative of glutamate. This last activity was subjected to ammonium sulfate fractionation and successive phenyl-Sepharose, DEAE-Sephacel, and Sephacryl S-200 HR column chromatography. A highly purified enzyme fraction was obtained. This new glutamate aminopeptidase had a molecular weight of 22 kDa and an optimum pH range of 7.2-8.0 and was inhibited by o-phenanthroline and bestatin.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
