الخلاصة

The first mammalian lectin was isolated by Gilbert Ashwell and Anatol Morell, meanwhile, firstmember of the ß-galactose-specific lectins family was isolated from the electric eel. The number of purified animal lectins has startedto grow quickly since the beginningof the 1980. Recently, studies directed to human were carried out concerning detection, purification, identification, determination of physical and chemical properties, as well as determination of lectins levels in the normal and abnormal individuals. The present study was designed to investigate lectins in sera of patients with kidney tumors, in addition to non tumoral kidney disease patients. Fifty five patients of malignant kidney tumors were enrolled in addition to 23 patients of benign kidney tumors, and 18 patients of non tumoral kidney diseases used as control groups, in addition to 46 healthy individuals were also investigated.The measurement of total serum proteins revealed significant (p < 0.001) decrease in patients of malignant tumors when compared with those of benign, non tumoral diseases, and healthy individuals. The conditionsof the hemagglutination assay of serum lectin activity were optimized. The cutoff value of the specific hemagglutination activity was found to equal 6 SHU for discriminatory malignant kidney tumors. Serum lectins activity were indicated to be inhibited bygalactose, mannose, lactose and N-acetyl galactosamine. Purification of lectin from sera of patients with malignant kidney tumors by affinity chromatography with the use of silver stain revealed LacBL PAGE of purified lectin demonstrated one band consisted lectin activity. These results suggest that the diagnosis of the specific hemagglutination activity of lectin is promising biomarker for discrimination of malignant kidney tumor patients and the purified lectin could be introduced in the field of biomarkers