Purification, and properties of a base non-specific acid ribonuclease from bullfrog (Rana catesbeiana).
An acid ribonuclease (RNase RCL2) was purified to homogeneity on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) from a homogenate of bullfrog liver (Rana catesbeiana). The apparent molecular weight estimated from SDS-PAGE was ca. 25kDa. The pH optimum of the RNase was 5.0. The RNase released mononucleotides from RNA in the order of 3'-UMP, 3'-GMP and 3'-AMP. The N-terminal amino acid sequence of RNase RCL2 was determined up to the 20th residue, and it was found to have a 5 residue sequence homology with that of oyster acid RNase [H. Watanabe et al. J. Biochem. (Tokyo), 114, 800 (1993)]. Thus, RNase RCL2 seems to be a member of the RNase T2 family RNases. This is the first evidence of the RNase T2 family RNase in amphibians.
Yagi
H
H
Department of Microbiology, College of Pharmacy, Nihon University, Chiba, Japan.
Kobayashi
H
H
Inokuchi
N
N
Koyama
T
T
Irie
M
M
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011892:Rana catesbeiana; D012260:Ribonucleases / Q000302:isolation & purification* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D012260:Ribonucleases