Results 161 to 170 of about 14,129 (184)
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Molecular aggregation of bovine pancreatic ribonuclease induced by substrate
Archives of Biochemistry and Biophysics, 1970Abstract The interaction between bovine cytidine-2′,3′-cyclic phosphate pancreatic ribonuclease and ribonucleic acid or cytidine-2′,3′-cyclic phosphate is studied by means of the gel-filtration method. The formation of a molecular aggregate of the enzyme as a function of time is shown.
A, Marzotto, L, Galzigna
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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.
L G, Chavez, H A, Scheraga
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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 ...
A A, Fedorov +5 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
J, Matousek +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
J, Matousek +4 more
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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.
D M, Rothwarf, H A, Scheraga
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Proline Isomerization in Bovine Pancreatic Ribonuclease A. 1. Unfolding Conditions
Biochemistry, 1998The slow fluorescence unfolding phase of bovine pancreatic ribonuclease A is studied by stopped-flow kinetics and site-directed mutagenesis of tyrosines to phenylalanine and prolines to alanine. It is shown conclusively that this phase arises from two specific sources: Tyr92 reporting on the cis-trans isomerization of Pro93 and Tyr115 reporting on the ...
D, Juminaga +2 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,
K P, Nambiar +3 more
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Regeneration of bovine pancreatic ribonuclease A. 1. Steady-state distribution
Biochemistry, 1993The regeneration of bovine pancreatic ribonuclease A (RNase A) from the reduced to the native form with mixtures of oxidized and reduced dithiothreitol has been studied at 25 degrees C, pH 8.0, by using a variety of current experimental techniques, including quenching the regeneration reaction with 2-aminoethyl methanethiosulfonate, fractionation of ...
D M, Rothwarf, H A, Scheraga
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A semisynthetic bovine pancreatic ribonuclease containing a unique nitrotyrosine residue
Archives of Biochemistry and Biophysics, 1985A fully active semisynthetic ribonuclease, RNase 1-118:111-124, may be prepared by enzymatically removing six residues from the COOH terminus of the protein (positions 119-124) and then complementing the inactive RNase 1-118 with a chemically synthesized peptide containing the COOH-terminal 14 residues of the molecule (RNase 111-124) [M. C.
D M, Sasaki +4 more
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Denaturations studies on bovine pancreatic ribonuclease
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983Amara J. Sagar, M.W. Pandit
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