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  • 标题:SITE-SPECIFIC DEUTERATION OF TYROSINE AND THEIR ASSAY BY SELECTIVE ION MONITORING METHOD
  • 本地全文:下载
  • 作者:Sachiko TOKUHISA ; Kumiyo SAISU ; Haruhisa YOSHIKAWA
  • 期刊名称:Journal of Nutritional Science and Vitaminology
  • 印刷版ISSN:0301-4800
  • 电子版ISSN:1881-7742
  • 出版年度:1980
  • 卷号:26
  • 期号:1
  • 页码:77-85
  • DOI:10.3177/jnsv.26.77
  • 出版社:Center for Academic Publications Japan
  • 摘要:L-[2', 3', 5', 6'-d]Tyrosine (Tyr-d4) and L-[2', 6'-d]Tyr (Tyr-d2) were prepared. Tyr was heated in conc. DCl at 180°C for 4 hr to obtain DL-[2, 2', 3', 5', 6'-d]Tyr '(Tyr-d5), then the deuterium on the 2-position of the compound was successfully replaced with proton by refluxing with an acetic acid-acetic anhydride mixture. The isotopic purity of DL-Tyr-d4 was about 60%. The racemic mixture was resolved enzymatically. L-Tyr-d2 was prepared by refluxing the resultant Tyr-d4 with 5.5 N HCI. The deuterated amino acids were analyzed as the N, O -bis (trifluoroacetyl) methyl ester or N, O -bis(heptafluorobutyryl) methyl ester derivatives by the gas chromatography-selective ion monitoring method (SIM). The calibration curves showed good linearity in the range where the molar ratios of Tyr-d4/Tyr-do and Tyr-d2/Tyr-do were above 5/1, 000. The results indicate that the protein-bound Tyr-d4 may possibly be determined as Tyr-d2 after hydrolysis of protein.
  • 关键词:tyrosine;gas chromatography-mass spectrometry;selective ion monitoring;deuterium;labeling
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