化学学报 ›› 2000, Vol. 58 ›› Issue (8): 1037-1042. 上一篇    下一篇

研究论文

火菇素酪氨酸微区的研究

冯永君;李德舜;孙丽;张长铠;蔺存国   

  1. 山东大学微生物技术国家重点实验室;山东大学化学学院.济南(250100)
  • 发布日期:2000-08-15

Studies on the tyrosine environment of flammulin

Feng Yongjun;Li Deshun;Sun Li;Zhang Changkai;Lin Cunguo   

  1. Shandong Univ., College of Chem.Jinan(250100)
  • Published:2000-08-15

用紫外差光谱和荧光光谱技术对火菇素的酪氨酸微区进行了研究,结果表明火菇素表现典型的酪氨酸残基紫外275nm吸收峰,ε~m~a~x=20322L·mol^-^1·cm^-^1,紫外差光谱滴定发现,当10.1

关键词: 火菇素, 酪氨酸, 荧光分光光度法, 紫外差示光谱

By the UV difference spectrum and fluorescence spectrum technique, the tyrosine environment of flammulin was studied and the results show a typical maximal UV absorption peak of tyrosine residues in flammulin at 275nm, with ε~ m~a~x=20322 L·mol^-^1·cm^-^1. According to the results of the UV difference spectrophotometric titration, the UV difference absorption △A~2~9~4~.~4~n~m shows close correlation to pH ranging from 10.1 to 12.5. The titration curve of tyrosine shows that the apparent dissociation constant pK~a' of tyrosine is 11.4. Since no tryptophane is found in flammulin, the protein only shows the fluorescence of tyrosine residues. The fluorescence spectrum of flammulin shows that the maximal emission wavelength is at 305nm when excited at 280nm, which is sensitive to SDS and ph and quenchable by acrylamide but not by KI. The results indicate that the tyrosine residues of flammulin reside in the hydrophobic core, and the tyrosine residues, together with other hydrophobic amino acid residues in flammulin, form a stable non-polar hydrophobic environment.

Key words: TYROSINE, FLUOROSPECTROPHOTOMETRY

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