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本文比较了GAPDH,CM-GAPDH以及经紫外光照射并带有新荧光团的GAPDH的圆二色性光谱。在200—250毫微米区域三者基本相同,加入SDS也没有显著影响。在250—300区域光照酶的CD光谱与每分子带有2个NAD~+的GAPDH相似,加入SDS使酶在这一区域的CD光谱基本消失。在300—360毫微米光照酶与GAPDH-NADH络合物类似有一平缓的CD正峰。与后者不同的是,即使加入过量的SDS也不能使光照酶的这一平缓正CCD峰完全消失。这一事实指示新荧光团与肽链的结合是牢固的,它所处的微环境也是比较稳定的。
This article compares the circular dichroism spectra of GAPDH, CM-GAPDH, and GAPDH irradiated with UV light and with a new fluorophore. The three were similar in the 200-250 nm area with no significant effect on the addition of SDS. The CD spectra of Illuminase at 250-300 are similar to those of GAPDH with 2 NAD + per molecule. Addition of SDS added the CD spectra of the enzyme in this region almost disappeared. The 300-360 nm light enzyme has a gentle CD positive peak similar to the GAPDH-NADH complex. Unlike the latter, the addition of excess SDS does not allow this flat positive CCD peak of the enzyme to completely disappear. This fact indicates that the binding of the new fluorophore to the peptide chain is firm and the microenvironment in which it is located is also relatively stable.