Results 241 to 250 of about 433,059 (284)

Biological Function of Pancreatic Ribonuclease

Nature, 1969
The physiological function of this much studied pancreatic enzyme has been misunderstood. It is essential only in ruminants and certain other herbivores, where it has a special function.
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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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Regeneration of bovine pancreatic ribonuclease A. 1. Steady-state distribution.

Biochemistry, 1993
The 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 ...
D. Rothwarf, H. Scheraga
semanticscholar   +1 more source

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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Regeneration of bovine pancreatic ribonuclease A: detailed kinetic analysis of two independent folding pathways.

Biochemistry, 1998
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, proceeds through two separate pathways in which separate nativelike three ...
D. Rothwarf, Yue-Jin Li, H. Scheraga
semanticscholar   +1 more source

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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Degradation of double-stranded RNA by human pancreatic ribonuclease: crucial role of noncatalytic basic amino acid residues.

Biochemistry, 2003
Under physiological salt conditions double-stranded (ds) RNA is resistant to the action of most mammalian extracellular ribonucleases (RNases). However, some pancreatic-type RNases are able to degrade dsRNA under conditions in which the activity of ...
S. Sorrentino, M. Naddeo, A. Russo, G. D'alessio   +3 more
semanticscholar   +1 more source

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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