Comparative Base Specificity, Stability, and Lectin Activity of Two Lectins from Eggs of Rana catesbeiana and R. japonica and Liver Ribonuclease from R. catesbeiana

• Published in: Journal of biochemistry (Tokyo) Vol. 109; no. 5; pp. 786 - 790
• Main Authors: Okabe, Yukie, Katayama, Naoko, Iwama, Masanori, Watanabe, Hideaki, Ohgi, Kazuko, Irie, Masachika, Nitta, Kazuo, Kawauchi, Hiroaki, Takayanagi, Yoshio, Oyama, Fumitaka, Yasuko Abe, Koichl Titani, Okazaki, Taro, Inokuchi, Norio, Koyama, Takashi
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 01.05.1991
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Female; Fundamental and applied biological sciences. Psychology; Glycoproteins; Hydrogen-Ion Concentration; Kinetics; Lectins - chemistry; Lectins - metabolism; Liver - enzymology; Molecular Sequence Data; Ovum - metabolism; Proteins; Rana catesbeiana; Rana japonica; Ranidae; Ribonucleases - chemistry; Ribonucleases - metabolism; Sequence Homology, Nucleic Acid; Substrate Specificity; Temperature; Lectin; Stability; Enzyme; Liver; Amphibia; Homology; Primary structure; Salientia; Ribonuclease; Vertebrata; Enzymatic activity; Substrate specificity; Agglutination; Kinetics; Rana catesbeiana
• ISSN: 0021-924X; 1756-2651
• DOI: 10.1093/oxfordjournals.jbchem.a123457

Two lectins with RNase activity obtained from eggs of Rana catesbeiana and R. japonica and RNase obtained from R. catesbeiana liver show 65–83% protein homology. The base specificity of these frog proteins was studied with 8 dinucleoside phosphates as substrates and 8 nucleotides as inhibitors. The base specificities of the B1 and B2 sites of these proteins are U>C and G>U>A, C, respectively. The three frog proteins are more resistant than RNase A to heat treatment, guanidine-HCl and pH-induced denaturation; i.e.,they retain their native conformation up to at least 70°C at pH 7.5. Differences in stability and base specificity among RNase A and the three frog proteins are discussed in relation to the primary structures. Although the two lectins agglutinate tumor cells (e.g., Ehrlich, S-180 and AH109A ascites carcinoma cells), the liver RNase has no such activity. Agglutination of AH109A cells by the two lectins is inhibited by nucleotides. Our results indicate that the agglutination sites are not identical with, but are related to, the active sites of the three frog proteins.