Pepys M B, De Beer F C, Milstein C P, March J F, Feinstein A, Butress N, Clamp J R, Taylor J, Bruton C, Fletcher T C
Biochim Biophys Acta. 1982 May 21;704(1):123-33. doi: 10.1016/0167-4838(82)90139-x.
C-reactive protein and serum amyloid P component were isolated from serum of the plaice (Pleuronectes platessa L.), a murine teleost. The isolation was based on their calcium-dependent binding affinity for pneumococcal C-polysaccharide and for agarose, respectively. These specificities are the same as those of human C-reactive protein and serum amyloid P component, respectively, and we have previously reported that the plaice molecules resemble human C-reactive protein and serum amyloid P component in their electron microscopic appearance. We describe here estimation of the molecular weights of plaice C-reactive protein and serum amyloid P component and their subunits, and analysis of their amino acid composition, glycosylation and partial amino-terminal amino acid sequences. The results establish that plaice C-reactive protein and serum amyloid P component are homologous with each other and with their human counterparts and indicate that there has been stable conservation of this protein family throughout vertebrate evolution.
从一种鼠类硬骨鱼——鲽（Pleuronectes platessa L.）的血清中分离出了C反应蛋白和血清淀粉样蛋白P成分。分离是基于它们分别对肺炎球菌C多糖和琼脂糖的钙依赖性结合亲和力。这些特异性分别与人C反应蛋白和血清淀粉样蛋白P成分的特异性相同，并且我们之前曾报道，鲽的这些分子在电子显微镜外观上类似于人C反应蛋白和血清淀粉样蛋白P成分。我们在此描述了鲽C反应蛋白和血清淀粉样蛋白P成分及其亚基的分子量估计，以及它们的氨基酸组成、糖基化和部分氨基末端氨基酸序列分析。结果表明，鲽C反应蛋白和血清淀粉样蛋白P成分彼此同源，且与它们的人类对应物同源，这表明在整个脊椎动物进化过程中，这个蛋白质家族一直保持着稳定的保守性。
