Two kinds of new lectin fractions (LOA-I, LOA-II) were obtained from loach (Misgurnus spp.) meat by 0.15 M NaCl extraction, salt fractionation, ion exchange and hydroxyapatite column chromatographies. On polyacrylamide gel electrophoresis, LOA-I exhibited one major and a few minor bands, but LOA-II exhibited three minor bands. The partially purified loach lectins agglutinated not only erythrocytes of human B and AB type, rabbit, dog, but also murine splenic lymphocytes. Agglutinability was relatively labile at various pH and stable at increasing temperature, but was not affected by tested several metal ions. By the sugar specificity test, D-glucosamine and metyl-$eta$-galactopyranose inhibited agglutinating activity at a final concentration of 3 mM. The lectins contained relatively high amounts of aspartic acid, valine and leucine, but sulfur containing amino acids, cystein, methionine and isoleucine were not determined. LOA-I, LOA-II lectins were nonmitogenic toward murine lymphocytes.