Brennan S O, Carrell R W
Biochim Biophys Acta. 1980 Jan 24;621(1):83-8. doi: 10.1016/0005-2795(80)90064-1.
Proalbumin Christchurch is a varient of human albumin in which the C-terminal basic residue of the propeptide has undergone a mutation to glutamine. In this investigation spectral and equilibrium dialysis studies have shown that the variant lacks the high affinity copper binding site of normal albumin. A simple electrophoretic procedure is described using 63Ni(II), which allow discrimination of proalbumins from other variants of albumin. The finding that Proalbumin Christchurch is readily cleaved in vitro by trypsin but is secreted uncleaved in vivo is evidence that propeptide cleavage is due to specific proteolysis with paired basic residues being a pre-requisite.
克赖斯特彻奇前清蛋白是人类白蛋白的一种变体，其中前肽的C末端碱性残基已突变为谷氨酰胺。在本研究中，光谱和平衡透析研究表明，该变体缺乏正常白蛋白的高亲和力铜结合位点。描述了一种使用63Ni(II)的简单电泳方法，该方法可将前清蛋白与白蛋白的其他变体区分开来。克赖斯特彻奇前清蛋白在体外易被胰蛋白酶切割，但在体内分泌时未被切割，这一发现证明前肽切割是由于特定的蛋白水解作用，成对的碱性残基是先决条件。
