Hamazaki H
Department of Biology, Kitasato University School of Medicine, Kanagawa, Japan.
Biochim Biophys Acta. 1990 Mar 1;1037(3):435-8. doi: 10.1016/0167-4838(90)90047-j.
Human serum amyloid P component (SAP) was digested with pronase P and a glycopeptide fraction was obtained by gel-permeation chromatography. Carbohydrate and amino-acid composition of the glycopeptide suggested that each subunit of SAP possesses an N-linked glycan, but no O-linked ones. The N-linked oligosaccharide of SAP was obtained by hydrazynolysis. The structure of the oligosaccharide, which was deduced by sequential digestion with exoglycosidases and subsequent gel filtration, was identical or very similar to that of human transferrin. Removal of sialic acids from SAP reduced the calcium-dependent binding activity for agarose by 7%, suggesting the terminal sialic acids were partially responsible for the binding.
人血清淀粉样蛋白P成分（SAP）用链霉蛋白酶P消化，并通过凝胶渗透色谱法获得糖肽组分。糖肽的碳水化合物和氨基酸组成表明，SAP的每个亚基都具有一个N-连接聚糖，但没有O-连接聚糖。通过肼解获得了SAP的N-连接寡糖。通过外切糖苷酶顺序消化和随后的凝胶过滤推断出的寡糖结构与人转铁蛋白的结构相同或非常相似。从SAP中去除唾液酸使琼脂糖的钙依赖性结合活性降低了7%，表明末端唾液酸部分负责这种结合。
