Lectins are non-immune origin proteins or glycoproteins binding to specific carbohydrate in the cell, that have been widely used as probes in cytochemical and oncological studies. The author investigated the lectin binding pattern in the histologically normal epithelium of the human larynx. Using the enzyme histochemical method with avidin-biotin-peroxidase complex(ABC), which is applicable to formalin fixed paraffin embedded tissue sections, the binding patterns of seven lectins were investingated:Concanavalin A(Con A), Wheat germ agglutinin(WGA), Ricinus communis agglutinin(RCA-1). Soybean agglutinin(SBA), Peanut agglutinin(PNA), Ulex europaeus agglutinin(UEA-1), Dolichos biflorus agglutinin(DBA). The results observed under the light microscope were as follows : 1) The specificity of the lectin binding in the laryngeal epithelium was confirmed with control experiments. No lectin showed a positive binding reaction to all of epithelial cells, and DBA lectin showed a negative binding reaction in the laryngeal epithelium. In the columnar epithelium, the lectin binding showed no different pattern between the supraglottic and subglottic region. 2) In the squamous epithelium, Con A and RCA-l lectins showed positive binding reactions to the basal cell layer ; Con A, WGA, RCA-1, SBA, and UEA-l lectins showed positive binding reactions to the spinous cell layer ; and Con A, WGA, and UEA-1 lectins showed positive binding reactions to the granular cell layer. In the columnar epithelium. SBA, PNA, and UEA-l lectins showed positive binding reactions to the basal cell layer. Six lectins, the exception was DBA, showed postive binding reactions to the ciliated cell layer with several intensities. Further studies of lectin precancerous lesions of the larynx and in laryngeal cancer, such as, the study to develop an early diagnostic and prognostic marker of laryngeal cancer. Could be continued from the results of this study.