Results 271 to 280 of about 22,977 (294)

Antigenic reactivity of artiodactyl pancreatic ribonucleases with antiserum to cow ribonuclease A

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1976
Abstract The antigenecity of six pancreatic ribonucleases differing up to 11% in amino acid sequence, and of a synthetic cow ribonuclease fragment (residues 1–14) was determined with antiserum to cow ribonuclease A, using the modified phage technique.
Gerda Groen, Gjalt W. Welling
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Stereochemistry of the transesterification step of pancreatic ribonuclease

Biochemical and Biophysical Research Communications, 1972
Summary Determination by X-ray analysis of the absolute configuration of uridine 3′-O-thiophosphate methyl ester obtained by the reaction of uridine 2′,3′-O,O-cyclothiophosphate with pancreatic ribonuclease in aqueous methanol, establishes an inline mechanism for the transesterification reaction of this enzyme.
Fritz Eckstein, Wolfram Saenger, D. Suck
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A sensitive assay for pancreatic ribonuclease

Analytical Biochemistry, 1965
Abstract A convenient, rapid assay for pancreatic ribonuclease is based on the release of acid-soluble ultraviolet-absorbing products from polycytidylate. The sensitivity (ca. 10 μμg of ribonuclease) is comparable to the most sensitive assays available.
Georgianna Sandeen, Steven B. Zimmerman
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The inhibition of pancreatic ribonuclease by anionic polymers

Archives of Biochemistry and Biophysics, 1959
Abstract The inhibition of pancreatic ribonuclease by ten sulfate-containing polymers has been examined. Sulfated corn amylose (13.9% S) and sulfated polyvinyl alcohol (17.2% S) were the most effective compounds. With sulfated corn amylose the inhibition was shown to be of the competitive type.
Christine E. Wiley, J. Fellig
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Evolution of Pancreatic Ribonucleases

1977
Pancreatic ribonucleases form a group of homologous proteins found in considerable quantities in the pancreas of a number of mammalian taxa and of a few reptiles (Barnard, 1969; Beintema et al., 1973). The ribonuclease activity found in different species varies greatly.
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Semisynthetic studies on bovine pancreatic ribonuclease

International Journal of Peptide and Protein Research, 1984
The S‐peptide of the enzyme bovine pancreatic ribonuclease has been used as a model for covalent semisynthesis. Methods for side‐chain protection, enzymatic cleavage of the peptide chain at the level of the single arginine‐10 and for selective deprotection of the α‐carboxyl function of this residue, have been examined.
Mauro Tonellato, O. Buso, A. Lucchiari, C. Di Bello   +3 more
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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
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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
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THE PRIMARY STRUCTURE OF MUSKRAT PANCREATIC RIBONUCLEASE

International Journal of Peptide and Protein Research, 1976
Pancreatic ribonuclease from muskrat (Ondatra zibethica) was isolated and its amino acid sequence was determined from tryptic digests of the performic acid‐oxidized and the reduced and aminoethylated enzyme. The peptides have been positioned in the sequence by homology with other ribonucleases.
A.M. van den Berg, H. van Dijk, B. Sloots, Jacob Beintema, Wim Gaastra   +4 more
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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
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