Results 251 to 260 of about 433,059 (284)

Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. I. Reinvestigation of the histidine peak assignments.

Biochemistry, 1975
The deuterium exchange kinetics of the C(2) protons of the four histidine residues of native bovine pancreatic ribonuclease A have been followed at pH 6.5 and 8.0 by proton magnetic resonance spectroscopy (1H NMR).
J. Markley
semanticscholar   +1 more source

The ribonuclease activity of crystallized pancreatic deoxyribonuclease

Analytical Biochemistry, 1966
Abstract Chromatography of crystallized pancreatic DNase on DEAE-cellulose separates DNase of high specific activity from an inactive protein fraction and the bulk of RNase activity. The RNase fraction that resisted physical separation from DNase could be preferentially inactivated by iodoacetate.
Steven B. Zimmerman, D Sandeen
openaire   +3 more sources

Folding and unfolding kinetics of the proline-to-alanine mutants of bovine pancreatic ribonuclease A.

Biochemistry, 1996
Four single mutants (P42A, P93A, P114A, and P117A) of bovine pancreatic ribonuclease A (RNase A) in which each mutant has one of the four prolines of RNase A changed to alanine were prepared.
Robert W. Dodge, H. Scheraga
semanticscholar   +1 more source

Regeneration of bovine pancreatic ribonuclease A: identification of two nativelike three-disulfide intermediates involved in separate pathways.

Biochemistry, 1998
During the regeneration of bovine pancreatic ribonuclease A (RNase A) from the reduced to the native form with mixtures of oxidized and reduced dithiothreitol at 25 degrees C, pH 8.0, the disulfide-containing protein intermediates achieve a steady-state ...
D. Rothwarf, Yue-Jin Li, H. Scheraga
semanticscholar   +1 more source

Dinitrophenylation and inactivation of bovine pancreatic ribonuclease A

Archives of Biochemistry and Biophysics, 1965
Abstract The dinitrophenylation of bovine pancreatic ribonuclease A at pH 8.0, 15 °C is confined in its initial stages to the modification of lysine residues. The sites of attack are the α-amino group of the N-terminal lysine residue and the ϵ-amino groups of the lysine residues in positions 7 and 41. The most reactive amino group is that at position
Jadwiga H. Kycia, Mirjam Halmann, C.H.W. Hirs   +2 more
openaire   +3 more sources

A nuclear localization sequence endows human pancreatic ribonuclease with cytotoxic activity.

Biochemistry, 2004
Some members of the ribonuclease superfamily, such as Onconase, are cytotoxic to cancer cells. This is not the case for human pancreatic ribonuclease. This lack of cytotoxicity is probably a result of the inhibition exerted by the cytosolic ribonuclease ...
M. Bosch, A. Benito, M. Ribó, T. Puig, B. Beaumelle, M. Vilanova   +5 more
semanticscholar   +1 more source

Isolation and characterization of a human colon carcinoma-secreted enzyme with pancreatic ribonuclease-like activity.

Biochemistry, 1986
A ribonuclease was isolated from serum-free supernatants of the human colon adenocarcinoma cell line HT-29. It was purified by cation-exchange and C18 reversed-phase high-performance liquid chromatography.
R. Shapiro, J. Fett, D. J. Strydom, B. Vallée   +3 more
semanticscholar   +1 more source

Purification and characterization of human pancreatic ribonuclease

Biochemistry, 1981
A ribonuclease (RNase) has been isolated from normal human pancreas obtained upon autopsy. About 5 mg of RNase is normally recovered per kilogram of pancreas, equivalent to ca. 70% of the total activity and a 700-fold purification from the initial acidified extract.
Marc Elson, Joachim Ludwig Weickmann, Dohn G. Glitz   +2 more
openaire   +2 more sources

Retention of the cis proline conformation in tripeptide fragments of bovine pancreatic ribonuclease A containing a non-natural proline analogue, 5,5-dimethylproline

, 1999
Attention is focused on l-5,5-dimethylproline (dmP) as a substitute to lock l-proline (Pro) in a cis conformation in peptides and proteins, to prevent cis/trans isomerization when a protein with cis X-Pro peptide groups unfolds.
S. An, C. Lester, Jin-Lin Peng, Y. Li, D. Rothwarf, E. Welker, T. Thannhauser, Lianshan Zhang, and James P. Tam, H. Scheraga   +9 more
semanticscholar   +1 more source

Structural characterization of an analog of the major rate-determining disulfide folding intermediate of bovine pancreatic ribonuclease A.

Biochemistry, 1997
The major rate-determining step in the oxidative regeneration of bovine pancreatic ribonuclease A (RNase A) proceeds through des-[40-95] RNase A, a three-disulfide intermediate lacking the Cys40-Cys95 disulfide bond. An analog of this intermediate, [C40A,
J. Laity, C. Lester, S. Shimotakahara, D. Zimmerman, G. Montelione, H. Scheraga   +5 more
semanticscholar   +1 more source