Partial characterization of lectin binding sites of retinal photoreceptor outer segments and interphotoreceptor matrix.
Partial characterization of lectin binding sites of retinal photoreceptor outer segments and interphotoreceptor matrix.
复制标题
视网膜感光器外节和感光器间基质的凝集素结合位点的部分表征。
DOI：
10.1002/cne.902280214
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发表时间：
1984
期刊：
影响因子：
--
通讯作者：
Napier-Marshall,L
中科院分区：
文献类型：
--
作者：
Wood,JG;Besharse,JC;Napier-Marshall,L
我们已经使用细胞化学与外切糖苷酶消化和聚丙烯酰胺凝胶电泳部分表征凝集素结合位点的interphotoreceptor矩阵和感光外节。为了使试剂均匀进入制备的所有区域，我们使用了一种程序，在细胞化学分析之前，用乙醇钠蚀刻塑料切片。非洲爪蟾眼杯塑料包埋切片的神经氨酸酶预处理导致麦胚凝集素结合丧失，同时出现蓖麻凝集素与感光细胞间基质的结合。与此相反，麦胚凝集素结合的外节不改变的神经氨酸酶预处理。这些结果表明，麦胚凝集素结合位点的interphotoreceptormatrix是唾液酸糖缀合物和外节结合位点不是唾液酸糖缀合物。酶消化后，凝集素细胞化学的基质多肽分离聚丙烯酰胺凝胶电泳不确定一个可能的候选人，引起细胞化学染色模式。凝集素细胞化学的视网膜，其中interphotoreceptor矩阵已被提取不显示小麦胚芽凝集素结合位点的矩阵的损失。这些结果表明，主要的麦胚凝集素结合位点的interphotoreceptor矩阵尚未身份不明的sialoglycoconjugates。
We have used cytochemistry together with exoglycosidase digestion and polyacrylamide gel electrophoresis to partially characterize lectin binding sites of the interphotoreceptor matrix and of photoreceptor outer segments. In order to obtain uniform access of reagents to all regions of the preparation, we have used a procedure in which plastic sections are etched with sodium ethoxide prior to cytochemical analysis. Neuraminidase pretreatment of plastic‐embedded sections ofXenopus laeviseyecups leads to a loss of wheat germ agglutinin binding and a concomitant appearance ofRicinus communisagglutinin binding to the interphotoreceptor matrix. In contrast, wheat germ agglutinin binding to the outer segments is not altered by the neuraminidase pretreatment. These results suggest that wheat germ agglutinin binding sites of interphotoreceptor matrix are sialoglyconjugates and that outer segment binding sites are not sialoglycoconjugates. Enzyme digestions followed by lectin cytochemistry of matrix polypeptides separated by polyacrylamide gel electrophoresis do not identify a likely candidate to give rise to the cytochemical staining patterns. Lectin cytochemistry of retinas from which the interphotoreceptor matrix has been extracted do not show a loss of wheat germ agglutinin binding sites to the matrix. These results suggest that the major wheat germ agglutinin binding sites in the interphotoreceptor matrix are to as yet unidentified sialoglycoconjugates.