Comparative physical-chemical studies of mammalian arginases

Comparative biochemistry and physiology Pub Date : 1970-12-01 DOI:10.1016/0010-406X(70)90563-3

Helga Hirsch-Kolb, John P Heine, Helmut J Kolb, David M Greenberg

{"title":"Comparative physical-chemical studies of mammalian arginases","authors":"Helga Hirsch-Kolb, John P Heine, Helmut J Kolb, David M Greenberg","doi":"10.1016/0010-406X(70)90563-3","DOIUrl":null,"url":null,"abstract":"<div><ul><li>1.1. Liver arginase (E.C. 3.5.3.1) of various mammalian species (rat, mouse, dog, rabbit, pork, monkey) were partly purified and their isoelectric properties determined by carboxymethyl cellulose column chromatorgraphy and isoelectric focusing.</li><li>2.2. The ureotelic arginase can be divided into mainly two groups; (i) basic and (ii) slightly acidic or neutral proteins.</li><li>3.3. The two groups of arginases showed marked differences in the binding of Mn2+.</li><li>4.4. Only beef liver arginase could be activated by Co2+ and Ni2+, all other mammalian arginases were inhibited by these metal ions.</li><li>5.5. The molecular weights were found to range from 120,000–160,000 daltons.</li><li>6.6. High Michaelis constanta (6–20 mM) were obtained for all arginases studied.</li><li>7.7. Similarities were also found in the pH optima (pH 9·3–10·5) as well as the optimal Mn2+ concentration (40 mM) required to obtain maximal catalytic activity.</li></ul></div>","PeriodicalId":78189,"journal":{"name":"Comparative biochemistry and physiology","volume":"37 3","pages":"Pages 345-359"},"PeriodicalIF":0.0000,"publicationDate":"1970-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0010-406X(70)90563-3","citationCount":"69","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Comparative biochemistry and physiology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0010406X70905633","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}

引用次数: 69

Abstract

1.
1. Liver arginase (E.C. 3.5.3.1) of various mammalian species (rat, mouse, dog, rabbit, pork, monkey) were partly purified and their isoelectric properties determined by carboxymethyl cellulose column chromatorgraphy and isoelectric focusing.
2.
2. The ureotelic arginase can be divided into mainly two groups; (i) basic and (ii) slightly acidic or neutral proteins.
3.
3. The two groups of arginases showed marked differences in the binding of Mn²⁺.
4.
4. Only beef liver arginase could be activated by Co²⁺ and Ni²⁺, all other mammalian arginases were inhibited by these metal ions.
5.
5. The molecular weights were found to range from 120,000–160,000 daltons.
6.
6. High Michaelis constanta (6–20 mM) were obtained for all arginases studied.
7.
7. Similarities were also found in the pH optima (pH 9·3–10·5) as well as the optimal Mn²⁺ concentration (40 mM) required to obtain maximal catalytic activity.

查看原文本刊更多论文

哺乳动物精氨酸酶的比较理化研究

1.1. 对不同哺乳动物(大鼠、小鼠、狗、兔、猪、猴)的肝精氨酸酶(E.C. 3.5.3.1)进行了部分纯化，并采用羧甲基纤维素柱层析和等电聚焦法测定了其等电性质。输尿管精氨酸酶主要分为两类;(i)碱性和(ii)微酸性或中性蛋白质。两组精氨酸酶对Mn2+.4.4的结合有显著差异。只有牛肝精氨酸酶能被Co2+和Ni2+激活，其他所有哺乳动物精氨酸酶均被这两种金属离子抑制。分子量在120,000-160,000道尔顿之间。所有精氨酸酶均获得高Michaelis constanta (6-20 mM)。获得最大催化活性所需的最佳pH值(pH 9.3 ~ 10.5)和最佳Mn2+浓度(40 mM)也存在相似之处。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文求助全文

来源期刊

Comparative biochemistry and physiology

自引率

0.00%

发文量