Reed R G, Peters T, Brennan S O, Carrell R W
Biochem J. 1980 Oct 1;191(1):281-3. doi: 10.1042/bj1910281.
Proalbumin Christchurch, a circulating variant of human serum albumin, is secreted from the liver without cleavage of the hexapeptide situated at the N-terminal end of the peptide chain of proalbumin. We compared ligand-binding properties of proalbumin Christchurch and of normal albumin A from the same individual in order to test the effect of the presence of the hexapeptide. The two albumin forms exhibited similar affinities for palmitate, bilirubin, 8-anilinonaphthalene-1-sulphonate and Bromocresol Green. The patterns of endogenous fatty acids bound to the two forms of albumin were slightly different, although the differences were probably not of physiological significance. From these studies it would appear that the propeptide of proalbumin does not alter the protein conformation in such a way as to alter binding sites for organic anions.
克赖斯特彻奇前清蛋白是人类血清白蛋白的一种循环变体，它由肝脏分泌，其前清蛋白肽链N端的六肽未被切割。我们比较了来自同一个体的克赖斯特彻奇前清蛋白和正常白蛋白A的配体结合特性，以测试六肽存在的影响。这两种白蛋白形式对棕榈酸、胆红素、8-苯胺基萘-1-磺酸盐和溴甲酚绿表现出相似的亲和力。与两种形式白蛋白结合的内源性脂肪酸模式略有不同，尽管这些差异可能没有生理意义。从这些研究看来，前清蛋白的前肽不会以改变有机阴离子结合位点的方式改变蛋白质构象。
