Sakata S
Nihon Seirigaku Zasshi. 1978;40(1):1-11.
An accessibility of the disulfide bonds of defatted SH-blocked bovine plasma albumin (BPA) to reduction by dithiothreitol was studied at 4 degree C. Upon reduction SH-blocked BPA acquired one SH per mole in the pH range from 4.0 to 6.0. Above pH 6.5 (the pH range of the N-B transition) an increasing number of the disulfide bonds became susceptible to reduction by dithiothreitol. Chemicals, such as KC1, fatty acid, sodium dodecylsulfate which suppress the structural fluctuation of BPA in the alkaline region decreased the accessibility of the disulfide bonds to reduction. The conversion of buried disulfide bonds into exposed ones is interpreted as being due to conformational changes in the N-B transition (pH 7.0 approximately 9.0).
在4℃下研究了脱脂的SH-封闭牛血浆白蛋白（BPA）的二硫键被二硫苏糖醇还原的可及性。还原后，在pH值为4.0至6.0的范围内，SH-封闭的BPA每摩尔获得一个SH。在pH 6.5以上（N-B转变的pH范围），越来越多的二硫键变得易于被二硫苏糖醇还原。诸如KCl、脂肪酸、十二烷基硫酸钠等抑制BPA在碱性区域结构波动的化学物质降低了二硫键还原的可及性。埋藏的二硫键向暴露的二硫键的转变被解释为是由于N-B转变（pH 7.0约9.0）中的构象变化所致。
