Gussakovsky E E, Haas E
Department of Life Sciences, Bar Ilan University, Ramat Gan, Israel.
FEBS Lett. 1992 Aug 17;308(2):146-8. doi: 10.1016/0014-5793(92)81263-l.
Reduced bovine pancreatic trypsin inhibitor (BPTI) has been shown to be in a compact state [(1988) Biochemistry 27, 8889-8893]. This leads to the proposal that this compact state may be a compact molten globule folding intermediate. Optical rotatory dispersion in the visible region failed to show the presence of pronounced secondary structures in the reduced BPTI and no binding of 8-anilino-1-naphthalenesulphonic acid to reduced BPTI could be detected. Yet, no cooperative thermal transition was detected by tyrosine fluorescence. These experiments show that reduced BPTI is not in the compact molten globule state.
已证明还原型牛胰蛋白酶抑制剂(BPTI)处于紧密状态[(1988年)《生物化学》27卷,8889 - 8893页]。由此提出这种紧密状态可能是一种紧密的熔球折叠中间体。在可见光区域的旋光色散未能显示还原型BPTI中存在明显的二级结构,并且未检测到8 - 苯胺基 - 1 - 萘磺酸与还原型BPTI的结合。然而,通过酪氨酸荧光未检测到协同热转变。这些实验表明还原型BPTI不处于紧密熔球状态。