Results 151 to 160 of about 14,129 (184)

First demonstration of lactoribonuclease, a ribonuclease from bovine milk with similarity to bovine pancreatic ribonuclease

Life Sciences, 2000
The isolation of a ribonuclease designated lactoribonuclease, with a molecular weight and an N-terminal amino acid sequence identical to those of bovine pancreatic ribonuclease, was first reported from bovine milk. After removal of globulin from acid whey by precipitation with 1.8 M (NH4)2SO4, (NH4)2SO4 was added to attain a concentration of 3.6 M ...
X Y, Ye, T B, Ng
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Conformational Flexibility of Bovine Pancreatic Ribonuclease A

Journal of the Physical Society of Japan, 1983
Conformational energies of native ribonuclease A were computed in the multi-dimensional space of dihedral angles of the backbone and side chains. By minimization of the total energy starting from three sets of the angles, we obtained three low energy conformations, C1, C2 and C3, which have almost the same energy, -644±4 kcal/mol and are close to the ...
Shoji Ihara, Tatsuo Ooi
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Radiation-induced Aggregation of Bovine Pancreatic Ribonuclease

International Journal of Radiation Biology and Related Studies in Physics, Chemistry and Medicine, 1963
SummaryPurified 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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Chemical synthesis of bovine pancreatic ribonuclease A

Journal of the Chemical Society, Chemical Communications, 1980
Bovine pancreatic ribonuclease, which consists of 124 amino acids, was synthesized in a conventional manner by assembling relatively small 30-peptide fragments of established purity.
Haruaki Yajima, Nobutaka Fujii
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Calculations of the CD spectrum of bovine pancreatic ribonuclease

Biopolymers, 1997
CD spectra of bovine pancreatic ribonuclease A (RNase A) and its subtilisin-modified from (RNase S) have been calculated, based upon high-resolution structures from x-ray diffraction. All known transitions in the peptide and side-chain groups, especially the aromatic and disulfide groups, have been included.
G, Kurapkat, P, Krüger, A, Wollmer, J, Fleischhauer, B, Kramer, E, Zobel, A, Koslowski, H, Botterweck, R W, Woody   +8 more
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Mapping the stability clusters in bovine pancreatic ribonuclease A

Biopolymers, 2009
AbstractIn the present work, we have thermodynamically characterized the thermally induced unfolding of 20 variants of bovine pancreatic ribonuclease A (RNase A) to experimentally describe the residues and the regions that are critical for the stability of the enzyme.
Roger, Vilà, Antoni, Benito, Marc, Ribó, Maria, Vilanova   +3 more
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Chromatography of bovine pancreatic ribonuclease on carboxymethylcellulose columns

Analytical Biochemistry, 1962
Abstract 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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Production of mature bovine pancreatic ribonuclease in Escherichia coli

Gene, 1992
The coding sequence for the bovine pancreatic ribonuclease (RNase) precursor has been cloned and produced in Escherichia coli using the polymerase chain reaction (PCR) technique. A PCR amplification has been carried out utilizing as template the recombinant plasmid, pQR138, which contains the coding sequence for the RNase precursor, and primers that ...
A, Tarragona-Fiol, C J, Taylorson, J M, Ward, B R, Rabin   +3 more
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24 Bovine Pancreatic Ribonuclease

1971
Publisher Summary This chapter discusses the process of isolation, chromatography, structure, and molecular and catalytic properties of bovine pancreatic ribonuclease. At present there are three simple and widely used chromatographic procedures: (1) Hirs base their method on the carboxyl ion exchange resin IRC-50 with 0.2 M phosphate buffer pH 6.45 ...
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Platinated oligomers of bovine pancreatic ribonuclease: Structure and stability

Journal of Inorganic Biochemistry, 2015
The reaction between cis-diamminedichloroplatinum(II) (CDDP), cisplatin, a common anticancer drug, and bovine pancreatic ribonuclease (RNase A), induces extensive protein aggregation, leading to the formation of one dimer, one trimer and higher oligomers whose yields depend on cisplatin/protein ratio.
PICONE, DELIA, DONNARUMMA, FEDERICA, Ferraro G, RUSSO KRAUSS, IRENE, Fagagnini A, Gotte G, MERLINO, ANTONELLO   +6 more
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