CHARACTERIZATION OF POLY-C-PREFERENTIAL RIBONUCLEASE FROM CHICKEN LIVER

被引:17
作者
HAYANO, K
IWAMA, M
SAKAMOTO, H
WATANABE, H
SANDA, A
OHGI, K
IRIE, M
机构
[1] HOSHI COLL PHARM, DEPT MICROBIOL, 2-4-41 EBARA, SHINAGAWA KU, TOKYO 142, JAPAN
[2] AZABU UNIV, FAC PUBL HLTH, SAGAMIHARA, KANAGAWA 229, JAPAN
[3] HOSHI COLL PHARM, DIV PHARMACOPOEIA, SHINAGAWA KU, TOKYO 142, JAPAN
关键词
D O I
10.1093/oxfordjournals.jbchem.a124132
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Poly C preferential RNase previously reported by Levy and Karpetsky [J. Biol. Chem. 255, 2153-2159 (1980)] and Miura et al. [Chem. Pharm. Bull. 32, 4053-4060 (1984)] was extensively purified from chicken liver to homogeneity as determined by SDS-PAGE (RNase CL2). The poly C preference over poly U was slightly higher than that of bovine pancreatic RNase A. However, the kinetic constants for 8 dinucleoside phosphates, CpY and UpY (Y = one of A, G, U, and C) as substrates showed that RNase CL2 was preferential for cytidylic acid, but less so than RNase A, and the influence of Y base on the rate of hydrolysis of CpY or UpY was less marked than in the case of RNase A. The primary structure of RNase CL2 was determined. The molecular weight calculated from the sequence was 13,420. Comparison of the amino acid sequence of RNase CL2 with those of other vertebrate RNases showed that RNase CL2 is a member of the RNase A family, but is not a non-secretory RNase. It retains 3 disulfide bridges of RNase A, but Cys65-Cys72 of RNase A is missing. As for the active site, the amino acid residues of the P0 and P1 sites of RNase A are completely conserved. Among the B1 site components, Thr45 (RNase A numbering) is conserved, but Phe120 and Ser123 are substituted by Leu and Thr, respectively. Among the B2 site residues, Gln69, Asn71, and Glu111, are substituted by other amino acids.
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页码:156 / 162
页数:7
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