E. Der Terrossian, R. Kassab, L.A. Pradel, Nguyen Van Thoai
{"title":"Composition en acides amines de l'ATP: l-arginine phosphotransferase cristallisee","authors":"E. Der Terrossian, R. Kassab, L.A. Pradel, Nguyen Van Thoai","doi":"10.1016/0926-6593(66)90038-5","DOIUrl":null,"url":null,"abstract":"<div><p><em>Amino acid composition of crystalline ATP: <span>l</span>-arginine phosphotransferase</em></p><ul><li><span>1.</span><span><p>1. ATP: <span>l</span>-arginine phosphotransferase (EC 2.7.3.3) has been crystallized from lobster muscle. Its specific activity was found to be 210–230 μmoles of P transferred per min per mg protein.</p></span></li><li><span>2.</span><span><p>2. From the amino acids analysis performed with a yield of 97.56%, the lobster enzyme was shown to have the following composition: Asp 38, Glu 46, Arg 19, Lys 31, Thr 21, Ser 20, His 8, Pro 11, Try 2, Tyr 11, Phe 20, Gly 28, Ala 28, Val 22, Ile 20, Leu 33, Met 8, Cyś 6, amide-N 23.</p></span></li><li><span>3.</span><span><p>3. The calculated molecular weight is 42 150 and the specific volume 0.731 ml/g.</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":"1966-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90038-5","citationCount":"41","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/0926659366900385","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 41
Abstract
Amino acid composition of crystalline ATP: l-arginine phosphotransferase
1.
1. ATP: l-arginine phosphotransferase (EC 2.7.3.3) has been crystallized from lobster muscle. Its specific activity was found to be 210–230 μmoles of P transferred per min per mg protein.
2.
2. From the amino acids analysis performed with a yield of 97.56%, the lobster enzyme was shown to have the following composition: Asp 38, Glu 46, Arg 19, Lys 31, Thr 21, Ser 20, His 8, Pro 11, Try 2, Tyr 11, Phe 20, Gly 28, Ala 28, Val 22, Ile 20, Leu 33, Met 8, Cyś 6, amide-N 23.
3.
3. The calculated molecular weight is 42 150 and the specific volume 0.731 ml/g.