犊牛肠碱性磷酸酶活性丝氨酸周围的氨基酸序列

Lorents Engström
{"title":"犊牛肠碱性磷酸酶活性丝氨酸周围的氨基酸序列","authors":"Lorents Engström","doi":"10.1016/0926-6569(64)90271-8","DOIUrl":null,"url":null,"abstract":"<div><p>The dipeptides Asp-SER<sup>32</sup>P and Ser<sup>32</sup>P-Ala have been isolated from an acid hydrolysate of calf-intestinal alkaline phosphate (orthophosphoric monoester phosphohydrolase, EC 3.I.3.I), which had been <sup>32</sup>P-labelled on a serine residue at the active site, as described earlier. This shows that the amino acid sequence aroun the active serine is ASP-Ser<sup>32</sup>P-Ala. The peptides were identified by using an acid hydrolysate of crytalline ovalbumin the same unballed peptides as reference substances.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 79-84"},"PeriodicalIF":0.0000,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90271-8","citationCount":"25","resultStr":"{\"title\":\"The amino acid sequence around the reactive serine in calf-intestinal alkaline phosphatase\",\"authors\":\"Lorents Engström\",\"doi\":\"10.1016/0926-6569(64)90271-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The dipeptides Asp-SER<sup>32</sup>P and Ser<sup>32</sup>P-Ala have been isolated from an acid hydrolysate of calf-intestinal alkaline phosphate (orthophosphoric monoester phosphohydrolase, EC 3.I.3.I), which had been <sup>32</sup>P-labelled on a serine residue at the active site, as described earlier. This shows that the amino acid sequence aroun the active serine is ASP-Ser<sup>32</sup>P-Ala. The peptides were identified by using an acid hydrolysate of crytalline ovalbumin the same unballed peptides as reference substances.</p></div>\",\"PeriodicalId\":100170,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"volume\":\"92 1\",\"pages\":\"Pages 79-84\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-10-23\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6569(64)90271-8\",\"citationCount\":\"25\",\"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/0926656964902718\",\"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/0926656964902718","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 25

摘要

二肽Asp-SER32P和Ser32P-Ala是从小牛肠碱性磷酸盐(正磷酸单酯磷酸水解酶,EC 3.I.3.I)的酸水解产物中分离出来的,如前所述,二肽在活性位点的丝氨酸残基上进行了32p标记。这表明活性丝氨酸周围的氨基酸序列为ASP-Ser32P-Ala。用酸水解结晶卵清蛋白鉴定肽,同样的非球化肽作为对照物质。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
The amino acid sequence around the reactive serine in calf-intestinal alkaline phosphatase

The dipeptides Asp-SER32P and Ser32P-Ala have been isolated from an acid hydrolysate of calf-intestinal alkaline phosphate (orthophosphoric monoester phosphohydrolase, EC 3.I.3.I), which had been 32P-labelled on a serine residue at the active site, as described earlier. This shows that the amino acid sequence aroun the active serine is ASP-Ser32P-Ala. The peptides were identified by using an acid hydrolysate of crytalline ovalbumin the same unballed peptides as reference substances.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信