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首页> 美国卫生研究院文献>Plant Physiology >Immunocytochemical Localization of a Wheat Germ Lysozyme in Wheat Embryo and Coleoptile Cells and Cytochemical Study of Its Interaction with the Cell Wall
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Immunocytochemical Localization of a Wheat Germ Lysozyme in Wheat Embryo and Coleoptile Cells and Cytochemical Study of Its Interaction with the Cell Wall

机译：小麦胚芽溶菌酶在小麦胚和胚芽鞘细胞中的免疫细胞化学定位及其与细胞壁相互作用的细胞化学研究

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摘要

Among several wheat (Triticum aestivum L.) germ proteins able to lyse Micrococcus lysodeikticus, one lysozyme (W1A) was purified by ion-exchange chromatography, gel filtration, and preparative polyacrylamide gel electrophoresis. Polyclonal antibodies against this lysozyme were raised in rabbits. The in situ localization of W1A lysozyme was achieved by the indirect protein A-gold technique. Large amounts of W1A lysozyme were found in cell walls whereas intercellular spaces, cytoplasm, and organelles were nearly free of labeling. Specificity of labeling was assessed with several controls. In an attempt to detect the presence of binding sites, W1A lysozyme was complexed to colloidal gold. Particles were specifically distributed in large amounts over wheat embryo and coleoptile cell walls. The absence of labeling over isolated coleoptile cell walls treated with 0.1 and 0.4 molar potassium hydroxide for hemicellulose extraction indicated that W1A lysozyme binding sites were probably of hemicellulosic nature.
机译：通过离子交换色谱，凝胶过滤和制备型聚丙烯酰胺凝胶电泳，纯化了几种能够裂解溶氧微球菌的小麦胚芽蛋白（W1A）。在兔中产生了针对这种溶菌酶的多克隆抗体。 W1A溶菌酶的原位定位是通过间接蛋白质A-金技术实现的。在细胞壁中发现大量的W1A溶菌酶，而细胞间的空间，细胞质和细胞器几乎没有标记。标记的特异性通过几种对照进行评估。为了检测结合位点的存在，将W1A溶菌酶与胶体金复合。颗粒专门大量分布在小麦胚和胚芽鞘细胞壁上。在用0.1和0.4摩尔氢氧化钾处理半纤维素提取物的分离的胚芽鞘细胞壁上没有标记，表明W1A溶菌酶结合位点可能具有半纤维素性质。

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