Purification of chicken liver ribonucleases by affinity chromatography with UMP-Sepharose (nucleosides and nucleotides. LII).

Miura, Kazunobu; Inoue, Yasuhiko; Hashimoto, Yukari; Inoue, Atsuko; Ueda, Tohru

doi:10.1248/cpb.32.4054

Cited by 10 publications

(2 citation statements)

References 2 publications

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“…Levy et al described the presence of cytosine base-specific RNase from chicken liver [11]. Miura et al further purified this RNase [12], and later Hayano et al elucidated the…”

Section: Introductionmentioning

confidence: 99%

Biochemistry of frog ribonucleases

Irie

Nitta

Nonaka

1998

Cellular and Molecular Life Sciences (CMLS)

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Frogs have unique pyrimidine base-specific RNases, with structures similar to those of turtle, iguana and chicken RNases. Among the four frog RNases discussed here, three from Rana pipiens, R. catesbeiana and R. japonica oocyte cells show antitumour activity, and the latter two show lectin activity towards sialic acid-rich glycoproteins. In this review, (i) we compare their unique primary structures with respect to the 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 and the antitumour activities of the three frog RNases.

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“…Levy et al described the presence of cytosine base-specific RNase from chicken liver [11]. Miura et al further purified this RNase [12], and later Hayano et al elucidated the…”

Section: Introductionmentioning

confidence: 99%

Biochemistry of frog ribonucleases

Irie

Nitta

Nonaka

1998

Cellular and Molecular Life Sciences (CMLS)

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“…The Table I The figures in parentheses were obtained from the sequence. K5* 3.8 (4) 1.4 (I) 3.3 (3) 1.0 (I) 2.3 (3) 0.8 (I) 1.4 (I) 1.3 (I) 1.4 (I) 1.5 (2) 0.8 (I) 2.4 (2) 1.4 (I) 1.0 (l) (2) 1.2 (I) 1.0 (l) -(I) ( 5) 49 60-64 (I) 0.8 (I) 2.5 (2) 1.8 (2) 3.1 (3) 0.9 (1) 1.6 (2) 1.1 (I) 2.0 (2) To identify the alignment of these lysylendopeptidase pep tides further, the RCM RNase CL l fraction was cleaved with BrCN. 14 ) After elimination of excess reagent, the portion soluble in 50 mM trimethylamine-acetate buffer (pH 8.0) was fractionated by HPLC on a Capcellpak column (Fig.…”

Section: Primary Structure Of Rnase Elimentioning

confidence: 99%

Base Specificity and Primary Structure of Poly U-preferential Ribonuclease from Chicken Liver

Uchida

Hayano

Iwama

et al. 1996

Bioscience, Biotechnology, and Biochemistry

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The primary structure and base specificity of chicken liver RNase CL1 which has been reported by Miura et al. [Chem. Pharm. Bull., 32, 4053-4060 (1984)] as poly U-preferential RNase, were extensively studied. The sequence study of this enzyme and comparison of the amino acid sequence of the enzyme with homologous RNases from oyster and Drosophila melanogaster suggested that RNase CL1 consists of three peptides with 17, 19, and 163 amino acid residues. The amino acid sequence of these three peptides were identified. The two small peptides are joined to the large peptide by disulfide bridges. The amino acid sequence of RNase CL1 had 62 (31.2%) and 63 residues (31.6%) identical with oyster RNase and D. melanogaster RNase, respectively, and belongs to the RNase T2 family RNase. Reassessment of the base specificity of RNase CL1 found that it is guanylic acid, then uridylic acid-preferential, and not poly U preferential.

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