{"title":"剑麻(龙舌兰)蛋白水解酶在脱氧纤维素上的分离","authors":"K.F. Tipton","doi":"10.1016/0926-6569(64)90191-9","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Crude sisal extract has been fractionated into seven protein components by chromatography on DEAE-cellulose.</p></span></li><li><span>2.</span><span><p>2. Each component was shown to be essentially homogeneous on rechromatography on DEAE-cellulose and on gel filtration on Sephadex G 100.</p></span></li><li><span>3.</span><span><p>3. Five of the components were shown to have proteolytic activity toward casein and four had amidase activity toward α-benzoyl-<span>l</span>-arginine amide.</p></span></li><li><span>4.</span><span><p>4. Four of the active components were found to be inhibited by metal binding agents and di-isopropylphosphorofluoridate.</p></span></li><li><span>5.</span><span><p>5. None of the active components appeared to depend on a sulphydryl group for activity.</p></span></li><li><span>6.</span><span><p>6. The components differed in their specific activities, pH optima, and molelcular weights as indicated by gel filtration on Sephadex G 100.</p></span></li></ul></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 2","pages":"Pages 334-340"},"PeriodicalIF":0.0000,"publicationDate":"1964-11-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90191-9","citationCount":"5","resultStr":"{\"title\":\"Fractionation of proteolytic enzymes from sisal (Agave sisalanus) on deae-cellulose\",\"authors\":\"K.F. Tipton\",\"doi\":\"10.1016/0926-6569(64)90191-9\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. Crude sisal extract has been fractionated into seven protein components by chromatography on DEAE-cellulose.</p></span></li><li><span>2.</span><span><p>2. Each component was shown to be essentially homogeneous on rechromatography on DEAE-cellulose and on gel filtration on Sephadex G 100.</p></span></li><li><span>3.</span><span><p>3. Five of the components were shown to have proteolytic activity toward casein and four had amidase activity toward α-benzoyl-<span>l</span>-arginine amide.</p></span></li><li><span>4.</span><span><p>4. Four of the active components were found to be inhibited by metal binding agents and di-isopropylphosphorofluoridate.</p></span></li><li><span>5.</span><span><p>5. None of the active components appeared to depend on a sulphydryl group for activity.</p></span></li><li><span>6.</span><span><p>6. The components differed in their specific activities, pH optima, and molelcular weights as indicated by gel filtration on Sephadex G 100.</p></span></li></ul></div>\",\"PeriodicalId\":100170,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"volume\":\"92 2\",\"pages\":\"Pages 334-340\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-11-22\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6569(64)90191-9\",\"citationCount\":\"5\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926656964901919\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926656964901919","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 5
摘要
1.1. 粗剑麻提取物经deae纤维素层析得到7个蛋白质组分。在deae -纤维素上的再层析和Sephadex G 100.3.3上的凝胶过滤表明,每个组分基本上都是均匀的。其中5个组分对酪蛋白具有蛋白水解活性,4个组分对α-苯甲酰-l-精氨酸酰胺具有酶活性。发现四种活性成分被金属结合剂和二异丙基氟化磷抑制。这些活性成分似乎都不依赖于巯基的活性。在Sephadex g100上进行凝胶过滤,发现两种组分的比活性、最优pH值和分子量存在差异。