Results 141 to 150 of about 4,881 (174)
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Mapping the stability clusters in bovine pancreatic ribonuclease A
Biopolymers, 2009AbstractIn 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.
Antoni Benito +3 more
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Enhancement of Bovine Pancreatic Ribonuclease Activity by Mercaptoethanol
Science, 1978Incubation of ribonuclease with 0.1 M mercaptoethanol at p H 8.5 can increase the enzyme's hydrolytic activity toward cytidine 2′,3′-monophosphate (cyclic CMP) under standard assay conditions.
John B. Watkins, F. W. Benz
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24 Bovine Pancreatic Ribonuclease
1971Publisher 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 ...
Harold W. Wyckoff, Frederic M. Richards
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Location of the antigenic determinants of bovine pancreatic ribonuclease
Biochemistry, 1979Four antigenic regions of native bovine pancreatic ribonuclease have been located by using antibodies that react specifically with segments 1--13, 31--79, and 80--124. These antibodies were purified by affinity chromatography on columns to which these peptide segments were bound.
Lloyd G. Chavez, Harold A. Scheraga
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The role of lysine in the action of bovine pancreatic ribonuclease A
Biochemistry, 1976The involvement of lysine residues in the active site of pancreatic ribonuclease has been investigated by assessing (a) the degree of substrate and substrate analogue protection of individual lysine residues against acetylation, and (b) the individual contribution of remaining unacetylated lysine residues to the total catalytic activity of the enzyme ...
Bert Walter, Finn Wold
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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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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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Platinated oligomers of bovine pancreatic ribonuclease: Structure and stability
Journal of Inorganic Biochemistry, 2015The 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 +6 more
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Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1995
Angiogenin, a member of the pancreatic-like ribonuclease family with a special biological action (RISBAses), is a basic protein that induces blood vessel formation. Another member of these special ribonucleases, bovine seminal ribonuclease (BS RNase), displays biological properties, including aspermatogenic, embryotoxic, antitumor and immunosuppressive
Josef Soucek +4 more
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Angiogenin, a member of the pancreatic-like ribonuclease family with a special biological action (RISBAses), is a basic protein that induces blood vessel formation. Another member of these special ribonucleases, bovine seminal ribonuclease (BS RNase), displays biological properties, including aspermatogenic, embryotoxic, antitumor and immunosuppressive
Josef Soucek +4 more
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Expression of bovine pancreatic ribonuclease A in Escherichia coli
European Journal of Biochemistry, 1987A synthetic gene for bovine pancreatic ribonuclease A (RNase A) has been expressed in Escherichia coli as a fusion protein with β‐galactosidase linked by the tetrapeptide Ile‐Glu‐Gly‐Arg. RNase A was cleaved from the fusion using factor Xa, and the resulting product prufied and reconstituted. The isolated RNase A was chromatographically, catalytically,
Krishnan P. Nambiar +3 more
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Denaturations studies on bovine pancreatic ribonuclease
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983Exposure of ribonuclease (EC 3.1.27.5) to 5% trichloroacetic acid solution is found to partially inactivate the enzyme. This inactivation is a function of time of exposure to trichloroacetic acid and reaches a plateau of about 45% residual activity. Higher concentrations of trichloroacetic acid lead to greater inactivation.
Amara J. Sagar, M.W. Pandit
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