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Ionic Interactions in Crystalline Bovine Pancreatic Ribonuclease A,
Biochemistry, 1996Isomorphous crystals (space group P3(2)21) of bovine pancreatic ribonuclease A (RNase A) were prepared at a pH of 5.5 in a series of high salt conditions, where both the nature of the ions and the ionic strength varied: 80% ammonium sulfate (mu = 12.5); 8 M sodium formate (mu = 8.0); 3 M NaCl, 30% ammonium sulfate (mu = 7.0); 3 M CsCl, 30% ammonium ...
Elena V. Fedorov +5 more
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Chromatography of bovine pancreatic ribonuclease on carboxymethylcellulose columns
Analytical Biochemistry, 1962Abstract A convenient method for the chromatographic separation of bovine pancreatic ribonuclease on carboxymethylcellulose in an airless, thermostated, constant-flow column is described. The marked effects of temperature on the elution pattern are discussed.
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Regeneration of bovine pancreatic ribonuclease A. 2. Kinetics of regeneration
Biochemistry, 1993Analysis of the experimental data of the previous paper [Rothwarf, D. M., & Scheraga, H. A. (1993) Biochemistry (first of four papers in this issue)], using the method of Konishi et al. [Konishi, Y., Ooi, T., & Scheraga, H. A. (1981) Biochemistry 20, 3945-3955; Konishi, Y., Ooi, T., & Scheraga H. A.
David M. Rothwarf, Harold A. Scheraga
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Radiation-induced Aggregation of Bovine Pancreatic Ribonuclease
International Journal of Radiation Biology and Related Studies in Physics, Chemistry and Medicine, 1963SummaryPurified bovine pancreatic ribonuclease in aqueous solution at a concentration of 10 mg per millilitre aggregated when exposed to 60Co gammaradiation. Aggregation was demonstrated by Sephadex chromatography. The aggregation process was inhibited by oxygen and by chemical protective agents. In the presence of oxygen, partially oxidized, partially-
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The Active Site and Mechanism of Action of Bovine Pancreatic Ribonuclease
Nature, 1961Bovine pancreatic ribonuclease is the only enzyme for which the primary structure is known (Hirs, Moore and Stein, 1960; Smyth, Stein and Moore, 1962; Potts et al., 1962; Gross and Witkop, 1962). The nature of the secondary and tertiary structure is, as yet, little understood although models have been proposed (Scheraga, 1960; Parks, 1960; Panar and ...
D. G. Herries +4 more
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Role of Phe120 in the Activity and Structure of Bovine Pancreatic Ribonuclease A
Journal of Biochemistry, 1998Phenylalanine120 is a candidate residue juxtaposing catalytic His12 and His119 in ribonuclease A (RNase A). To clarify its role in construction of the catalytic center, Phe120 was replaced by alanine, tryptophan, leucine, or glutamic acid by site-directed mutagenesis.
Naoki Tanimizu +2 more
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Structure of Crystal Form IX of Bovine Pancreatic Ribonuclease A
Acta Crystallographica Section D Biological Crystallography, 1997The X-ray structure of crystal form IX of bovine pancre- atic ribonuclease A (space group P2(1)2(1)2(1)) is reported at 1.6 A resolution. The structure was refined to an R factor of 15.0% and includes coordinates for two sulfate ions, four methanol molecules and 82 waters.
Jeffrey A. Bell, M.H. Dung
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Isolation and characterization of monodeamidated derivatives of bovine pancreatic Ribonuclease A
International Journal of Peptide and Protein Research, 1984The isolation and characterization of the initial intermediates formed during the irreversible acid denaturation of enzyme Ribonuclease A are described. The products obtained when RNase A is maintained in 0.5 M HCl at 30° for periods up to 20 h have been analyzed by ion‐exchange chromatography on Amberlite XE‐64.
Paul J. Vithayathil, Yeldur P. Venkatesh
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Modification of amino acids and bovine pancreatic ribonuclease a by kethoxal
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1977Kethoxal (3-ethoxy-2-ketobutanal) reacts with the guanidino group of Nalpha-acetylarginine to produce four derivatives, reactive to periodate, stable at pH 7, with 15% reverting to arginine on acid hydrolysis. Other amino acids with blocked alpha-amino groups do not react, except the epsilon-amino of lysine (slowly). The pK of the mixed Kethoxal-Nalpha-
Herbert Iijima +2 more
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Modification of bovine pancreatic ribonuclease A with 6-chloropurine riboside
Archives of Biochemistry and Biophysics, 1986The chemical modification of bovine pancreatic ribonuclease A by 6-chloropurine riboside was studied to obtain information about the role of the purine nucleoside moiety of the ribonucleic acid in the enzyme-substrate interaction. The residues involved in the reaction were identified, after performic acid oxidation and trypsin digestion, by reverse ...
Juli Alonso +2 more
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