Boström S, Deinum J, Löfroth J E, Wirth M, Kubista M
Hässle Cardiovascular Research Laboratories, Mölndal, Sweden.
Thromb Res. 1990 Sep 1;59(5):851-8. doi: 10.1016/0049-3848(90)90398-v.
The protein conformation of latent and active PAI-1 has been studied with circular dichroism, absorbance and fluorescence spectroscopy. The far ultraviolet circular dichroism spectrum of latent PAI-1 displays a more negative band at 220 nm than active PAI-1, crossing the baseline at a lower wavelength. Active PAI-1 shows an absorption maximum at lower wavelength (269 nm) than present in latent PAI-1 (278 nm). In consistency, slow denaturation of active PAI-1 by incubation for two hours at 37 degrees C induces a shift in the absorption maximum from 268 nm to 274 nm. The fluorescence emission maximum of latent PAI-1 is at lower wavelength (335 nm) than that of active PAI-1 (340 nm). These spectroscopic differences are interpreted as reflecting a more tight conformation, with the tryptophan residues in a more apolar environment, in latent PAI-1 compared to active PAI-1.
已通过圆二色性、吸光度和荧光光谱法研究了潜伏型和活性型纤溶酶原激活物抑制剂-1（PAI-1）的蛋白质构象。潜伏型PAI-1的远紫外圆二色光谱在220nm处显示出比活性型PAI-1更负的谱带，在更低波长处穿过基线。活性型PAI-1在比潜伏型PAI-1（278nm）更低的波长（269nm）处显示出最大吸收。与此一致的是，活性型PAI-1在37℃孵育两小时进行缓慢变性会导致最大吸收波长从268nm移至274nm。潜伏型PAI-1的荧光发射最大值在比活性型PAI-1（340nm）更低的波长（335nm）处。这些光谱差异被解释为反映了与活性型PAI-1相比，潜伏型PAI-1具有更紧密的构象，色氨酸残基处于更非极性的环境中。
