Luz Bascur, Julio Cabello, Marta Véliz, Adriana González
{"title":"人肝精氨酸酶的分子形式","authors":"Luz Bascur, Julio Cabello, Marta Véliz, Adriana González","doi":"10.1016/0926-6593(66)90151-2","DOIUrl":null,"url":null,"abstract":"<div><p>The chromatography of liver homogenates and purified preparations of human-liver arginase (<span>l</span>-arginine ureohydrolase, EC 3.5.3.1) on CM-cellulose separates two protein fractions with arginase activity. On rechromatography, each of these fractions appears homogeneous and retains its adsorption-elution characteristics.</p><p>Both arginase fractions have similar properties as far as their affinities for substrates, pH optima and thermal inactivation are concerned. However, they differ in their pH stabilities and in their inhibition by ornithine and canavanine.</p></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 1","pages":"Pages 149-154"},"PeriodicalIF":0.0000,"publicationDate":"1966-10-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90151-2","citationCount":"36","resultStr":"{\"title\":\"Molecular forms of human-liver arginase\",\"authors\":\"Luz Bascur, Julio Cabello, Marta Véliz, Adriana González\",\"doi\":\"10.1016/0926-6593(66)90151-2\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The chromatography of liver homogenates and purified preparations of human-liver arginase (<span>l</span>-arginine ureohydrolase, EC 3.5.3.1) on CM-cellulose separates two protein fractions with arginase activity. On rechromatography, each of these fractions appears homogeneous and retains its adsorption-elution characteristics.</p><p>Both arginase fractions have similar properties as far as their affinities for substrates, pH optima and thermal inactivation are concerned. However, they differ in their pH stabilities and in their inhibition by ornithine and canavanine.</p></div>\",\"PeriodicalId\":100160,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation\",\"volume\":\"128 1\",\"pages\":\"Pages 149-154\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1966-10-17\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6593(66)90151-2\",\"citationCount\":\"36\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926659366901512\",\"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) - Enzymology and Biological Oxidation","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926659366901512","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The chromatography of liver homogenates and purified preparations of human-liver arginase (l-arginine ureohydrolase, EC 3.5.3.1) on CM-cellulose separates two protein fractions with arginase activity. On rechromatography, each of these fractions appears homogeneous and retains its adsorption-elution characteristics.
Both arginase fractions have similar properties as far as their affinities for substrates, pH optima and thermal inactivation are concerned. However, they differ in their pH stabilities and in their inhibition by ornithine and canavanine.
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