{"title":"编码人半乳糖-1-磷酸尿苷转移酶的cDNA序列。","authors":"J E Flach, J K Reichardt, L J Elsas","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>We report a revised sequence of a cDNA that encodes a human galactose-1-phosphate uridyl transferase. The cDNA is 1295 bases in length and encodes a 43,000 Mr protein. The sequence was derived from a cDNA clone isolated from a transformed human lymphoblast cell line and amplified in a polymerase chain reaction. The revised sequence reveals a higher degree of amino acid conservation between the human enzyme and the homologous enzymes from Escherichia coli and yeast than was previously thought to exist.</p>","PeriodicalId":77573,"journal":{"name":"Molecular biology & medicine","volume":"7 4","pages":"365-9"},"PeriodicalIF":0.0000,"publicationDate":"1990-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Sequence of a cDNA encoding human galactose-1-phosphate uridyl transferase.\",\"authors\":\"J E Flach, J K Reichardt, L J Elsas\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>We report a revised sequence of a cDNA that encodes a human galactose-1-phosphate uridyl transferase. The cDNA is 1295 bases in length and encodes a 43,000 Mr protein. The sequence was derived from a cDNA clone isolated from a transformed human lymphoblast cell line and amplified in a polymerase chain reaction. The revised sequence reveals a higher degree of amino acid conservation between the human enzyme and the homologous enzymes from Escherichia coli and yeast than was previously thought to exist.</p>\",\"PeriodicalId\":77573,\"journal\":{\"name\":\"Molecular biology & medicine\",\"volume\":\"7 4\",\"pages\":\"365-9\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1990-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Molecular biology & medicine\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Molecular biology & medicine","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Sequence of a cDNA encoding human galactose-1-phosphate uridyl transferase.
We report a revised sequence of a cDNA that encodes a human galactose-1-phosphate uridyl transferase. The cDNA is 1295 bases in length and encodes a 43,000 Mr protein. The sequence was derived from a cDNA clone isolated from a transformed human lymphoblast cell line and amplified in a polymerase chain reaction. The revised sequence reveals a higher degree of amino acid conservation between the human enzyme and the homologous enzymes from Escherichia coli and yeast than was previously thought to exist.
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