Frogs have unique pyrimidine base-specific RNases, with structures sim
ilar to those of turtle, iguana and chicken RNases. Among the four fro
g RNases discussed here, three from Rana pipiens, R. catesbeiana and R
. japonica oocyte cells show antitumour activity, and the latter two s
how lectin activity towards sialic acid-rich glycoproteins. In this re
view, (i) we compare their unique primary structures with respect to t
he locations of their disulphide bridges, three-dimensional structure,
base specificity and heat stability as compared with RNase A, and (ii
) we summarize current knowledge about the mode of action of lectin an
d the antitumour activities of the three frog RNases.