{"title":"大鼠肝脏脯氨酸- srna合成酶的一些性质","authors":"Clark Bublitz","doi":"10.1016/0926-6593(66)90153-6","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Some of the properties of a proline-sRNA synthetase from rat liver have been studied by either the hydroxamate assay or the proline-dependent <sup>32</sup>PP<sub>i</sub>-ATP exchange.</p></span></li><li><span>2.</span><span><p>2. The enzyme was noticeably stabilized by sucrose. Although all preparations were stimulated by mercaptoethanol, some aged preparations had an absolute requirement for added mercaptan for activity.</p></span></li><li><span>3.</span><span><p>3. The enzyme required either magnesium, manganese, or calcium for activity. Hydroxamate formation was inhibited by PP<sub>i</sub>.</p></span></li><li><span>4.</span><span><p>4. [<sup>14</sup>C]Proline hydroxamate formation was inhibited by 3,4-dehydroproline; azetidine carboxylic acid; thiazolidine carboxylic acid; 2-methyl-, 2-ethyl-, or 2-propylthiazolidine carboxylic acid; thiazolidine; and mercaptoethylamine. Thiazolidine and mercaptoethylamine were competitive inhibitors of proline.</p></span></li><li><span>5.</span><span><p>5. The specific activity of extracts from younger rats was higher than that from older rats. Starvation also increased the activity of the extracts.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"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)90153-6","citationCount":"9","resultStr":"{\"title\":\"Some properties of proline-sRNA synthetase from rat liver\",\"authors\":\"Clark Bublitz\",\"doi\":\"10.1016/0926-6593(66)90153-6\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. Some of the properties of a proline-sRNA synthetase from rat liver have been studied by either the hydroxamate assay or the proline-dependent <sup>32</sup>PP<sub>i</sub>-ATP exchange.</p></span></li><li><span>2.</span><span><p>2. The enzyme was noticeably stabilized by sucrose. Although all preparations were stimulated by mercaptoethanol, some aged preparations had an absolute requirement for added mercaptan for activity.</p></span></li><li><span>3.</span><span><p>3. The enzyme required either magnesium, manganese, or calcium for activity. Hydroxamate formation was inhibited by PP<sub>i</sub>.</p></span></li><li><span>4.</span><span><p>4. [<sup>14</sup>C]Proline hydroxamate formation was inhibited by 3,4-dehydroproline; azetidine carboxylic acid; thiazolidine carboxylic acid; 2-methyl-, 2-ethyl-, or 2-propylthiazolidine carboxylic acid; thiazolidine; and mercaptoethylamine. Thiazolidine and mercaptoethylamine were competitive inhibitors of proline.</p></span></li><li><span>5.</span><span><p>5. The specific activity of extracts from younger rats was higher than that from older rats. Starvation also increased the activity of the extracts.</p></span></li></ul></div>\",\"PeriodicalId\":100160,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation\",\"volume\":null,\"pages\":null},\"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)90153-6\",\"citationCount\":\"9\",\"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/0926659366901536\",\"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/0926659366901536","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Some properties of proline-sRNA synthetase from rat liver
1.
1. Some of the properties of a proline-sRNA synthetase from rat liver have been studied by either the hydroxamate assay or the proline-dependent 32PPi-ATP exchange.
2.
2. The enzyme was noticeably stabilized by sucrose. Although all preparations were stimulated by mercaptoethanol, some aged preparations had an absolute requirement for added mercaptan for activity.
3.
3. The enzyme required either magnesium, manganese, or calcium for activity. Hydroxamate formation was inhibited by PPi.
4.
4. [14C]Proline hydroxamate formation was inhibited by 3,4-dehydroproline; azetidine carboxylic acid; thiazolidine carboxylic acid; 2-methyl-, 2-ethyl-, or 2-propylthiazolidine carboxylic acid; thiazolidine; and mercaptoethylamine. Thiazolidine and mercaptoethylamine were competitive inhibitors of proline.
5.
5. The specific activity of extracts from younger rats was higher than that from older rats. Starvation also increased the activity of the extracts.
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