The Effect of Temperature, Enzymic Complex Formation on the Room-Temperature Phosphorescence of Tryptophan Residue in Horse Liver Alcohol Dehydrogenase

スポンサーリンク

概要

• 論文の詳細を見る

• The binding of NAD,' NADH and ADPR to LADH was accompaniedby different temperature dependence of the phosphorescence decay rate of thetryptophan residue buried within the protein over the temperature range 0 to30'C in aqueous solution. As a result of thermally induced transition with ahysteresis cycle in the response to temperature, the Arrhenius curves of thephosphorescence decay rate for NAD- and ADPR-Et0H-LADH complexeswere overlapped with those for NADH- and ADPR-LADH complexes, respec-tively. The typical Value of the decay rate at 0'C for the samples distributed atintervals over the range 20 -1.5 sec=' suggesting that the degree of stability ofLADH dimer decreased in the order NADH->NAD->[108->ADPR-LADH.In order to explain those results by thermal fluctuation process, a model for theconformation changes of the micro-environment around the residue is presented.

• 社団法人日本物理学会の論文
• 1980-03-15

著者

• Kai Yoshiyuki

  Department Of Physics Faculty Of Science Nagoya University

関連論文

• Phosphorescence of Ribonuclease T_1 in Solution at 293 K
• The Effect of Temperature, Enzymic Complex Formation on the Room-Temperature Phosphorescence of Tryptophan Residue in Horse Liver Alcohol Dehydrogenase

スポンサーリンク