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On the other hand, several similar RNases have been isolated from plants, such as RNase LE from cultured tomato cells ( Lycopersicon esculentum) 8,9 and from seeds of Cucurbitaceae plants such as bitter gourd, 10 cucumber, and melon, and their primary structures elucidated. 7 Thus RNase T2-like enzymes also exist in plants. RNases with similar structures were found in self-incompatibility factors of Nicotiania alata, encoded by an allelic S-gene, and it was further recognized that these factors have RNase activity. 4–6 They contained two unique sequences, CAS1 and CAS 2, which have amino acid residues present at the active site of the enzymes.
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2 and Horiuchi et al., 3 respectively, in 1988, and the primary structures of other fungal RNase T2-like enzymes have also been elucidated. The primary structures of RNase T2 and the similar enzyme, RNase Rh from Rhizopus niveus, were determined by Kawata et al. Thus, they were first thought to be typical fungal RNases. Many fungi and commercial digestives produced from fungi contain similar RNase T2-like RNases. 1 In contrast to RNase T1, which is an exclusively guanylic acid-specific RNase, RNase T2 is a base nonspecific acid RNase. RNase T2 was first isolated from a commercial digestive, Taka-diastase ( Aspergillus oryzae), along with RNase T1, by Sato and Egami. Masachika Irie, Kazuko Ohgi, in Methods in Enzymology, 2001 Classification