Tsutsui Shigeyuki, Yamamura Nozomi, Yoshida Takaya, Nakamura Osamu
School of Marine Biosciences, Kitasato University, 1-15-1 Kitasato, Sagamihara, Kanagawa 252-0373, Japan
School of Marine Biosciences, Kitasato University, 1-15-1 Kitasato, Sagamihara, Kanagawa 252-0373, Japan.
J Biochem. 2015 Sep;158(3):189-95. doi: 10.1093/jb/mvv033. Epub 2015 Mar 20.
A 40-kDa lectin with N-acetyl-d-glucosamine-binding ability was purified from the sera of fugu (Takifugu rubripes) by affinity chromatography and subsequent gel filtration. N-terminal amino acid sequencing, in silico cloning using the fugu genome database and cDNA cloning demonstrated that this lectin is a homologue of kalliklectin, a novel lectin that was previously found in the flathead teleost Platycephalus indicus and has structural similarity to mammalian plasma kallikreins and coagulation factor XI. This is the second report of a kalliklectin, but the fugu kalliklectin differs in its sugar-binding spectra, intersubunit association and tissue distribution from the previously identified flathead kalliklectin. These findings indicate that kalliklectins vary in properties among fish species.
通过亲和层析和随后的凝胶过滤，从河豚（红鳍东方鲀）血清中纯化出一种具有N-乙酰-d-葡萄糖胺结合能力的40 kDa凝集素。N端氨基酸测序、利用河豚基因组数据库进行的电子克隆以及cDNA克隆表明，这种凝集素是激肽凝集素的同源物，激肽凝集素是一种新型凝集素，先前在鲬形目硬骨鱼印度鲬中发现，与哺乳动物血浆激肽释放酶和凝血因子XI具有结构相似性。这是关于激肽凝集素的第二篇报道，但河豚激肽凝集素在糖结合谱、亚基间缔合和组织分布方面与先前鉴定的印度鲬激肽凝集素不同。这些发现表明，激肽凝集素在不同鱼类物种中的特性存在差异。
