Recognition molecules and immunoglobulin domains in invertebrates.
Recognition molecules and immunoglobulin domains in invertebrates.
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无脊椎动物中的识别分子和免疫球蛋白结构域。
DOI：
10.1111/j.1749-6632.1994.tb33563.x
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发表时间：
1994
影响因子：
5.2
通讯作者：
Marchalonis,JJ
中科院分区：
文献类型：
--
作者：
Schluter,SF;Schroeder,J;Wang,E;Marchalonis,JJ
我们使用特异的抗体探针来保守抗原基序，以鉴定和表征被毛类中的免疫球蛋白相关分子，以及在七鳃鳗中发现的与被毛类和哺乳动物中的分子相关的C型凝集素。被膜免疫球蛋白交叉反应分子(MU CRM)与鲨鱼免疫球蛋白重链抗体发生反应。完整的衣状物Mu CRM是Ig轻链亚基的单体，经IEF鉴定为寡克隆。免疫化学数据和多肽序列同源性均表明该分子与Ig有关。七鳃鳗凝集素是一种由35-kDa和60-kDa亚基组成的大分子聚合物。多肽序列同源性和活性对钙的需求表明，它可能与C型凝集素有关。相关分子似乎存在于被毛类和哺乳动物中，这从免疫印迹中的抗体与血淋巴和T细胞提取物的单条带的交叉反应中可以看出。
We have used specific antibody probes to conserved antigenic motifs to identify and characterize immunoglobulin-related molecules in tunicates and a C-type lectin found in lamprey that is related to molecules found in tunicates and mammals. The tunicate immunoglobulin cross-reactive molecule (mu CRM) reacts with antibodies raised to shark IgM heavy chains. Intact tunicate mu CRM is a monomer of Ig light-chain-sized subunits and is oligoclonal by IEF. That this molecule is related to Ig is indicated both by immunochemical data and by peptide sequence homologies. The lamprey lectin is a large polymer (> 500,000 kDa) of 35-kDa and 60-kDa subunits. It appears to be related to C-type lectins as shown by peptide sequence homology and the requirement of Ca2+ for activity. Related molecules appear to be present in tunicates and mammals as shown by cross-reactivity of antibodies in Western blots with single bands from hemolymph and T-cell extracts.