Results 231 to 240 of about 433,059 (284)
Some of the next articles are maybe not open access.
Explanation of the observation of pancreatic ribonuclease activity at pH 4.5.
International journal of peptide & protein research, 2009A recent conclusion that beef pancreas contained a molecular species of ribonuclease with intrinsically high activity at pH 4.5 has been found to be incorrect. The particular assay used in the earlier experiments gives anomalous results at acid pH in the
J. Bartholeyns +5 more
semanticscholar +1 more source
Bactericidal activity engineered on human pancreatic ribonuclease and onconase.
Molecular Pharmaceutics, 2009Ribonucleases belonging to the pancreatic-type family exhibit a variety of biological activities that make them potential candidates as chemotherapeutic agents.
G. Torrent +3 more
semanticscholar +1 more source
Ribonuclease of bovine milk: Serological relationship to pancreatic ribonuclease
Archives of Biochemistry and Biophysics, 1964Abstract Ribonuclease isolated from bovine milk has been shown to be serologically identical to pancreatic ribonuclease. The presence of ribonuclease in milk was demonstrated directly by a gel-diffusion method. The serological method employed did not detect ribonuclease in bovine serum.
Henry Stevens, E. J. Coulson
openaire +3 more sources
Studies on the primary structure of bison pancreatic ribonuclease.
International journal of peptide & protein research, 2009Bison pancreatic ribonuclease was isolated by affinity chromatography. Thermolysin and tryptic digestion of denaturated protein, and subtilisin digestion of native protein yielded peptides, which were purified and submitted to amino acid analysis.
F. Muskiet, G. Welling, J. Beintema
semanticscholar +1 more source
Serum Deoxyribonuclease and Ribonuclease in Pancreatic Cancer and Chronic Pancreatitis
Tumori Journal, 1985Serum ribonuclease (RNase) and deoxyribonuclease (DNase) were investigated in 18 control subjects, and in 22 patients with pancreatic cancer, 13 with chronic pancreatitis and 29 with extrapancreatic diseases in order to assess their clinical usefulness in pancreatic cancer diagnosis and to evaluate whether modifications were consensual and/or age ...
BASSO, DANIELA +7 more
openaire +4 more sources
Current protein and peptide science, 2008
Pancreatic-type ribonucleases are a family of RNA degrading enzymes that share different degrees of sequence identity but a very similar 3D-structure. The prototype of this family is bovine pancreatic ribonuclease or ribonuclease A.
A. Benito +3 more
semanticscholar +1 more source
Pancreatic-type ribonucleases are a family of RNA degrading enzymes that share different degrees of sequence identity but a very similar 3D-structure. The prototype of this family is bovine pancreatic ribonuclease or ribonuclease A.
A. Benito +3 more
semanticscholar +1 more source
1982
Publisher Summary Bovine Ribonuclease has been a test protein in the study of a wide variety of chemical and physical methods of protein chemistry. It is widely employed in the course of the sequencing of RNA. This chapter discusses the usefulness of the cytoplasmic inhibitor of RNase to protect RNA in the course of the synthesis of complementary DNA
Peter Blackburn, Stanford Moore
openaire +2 more sources
Publisher Summary Bovine Ribonuclease has been a test protein in the study of a wide variety of chemical and physical methods of protein chemistry. It is widely employed in the course of the sequencing of RNA. This chapter discusses the usefulness of the cytoplasmic inhibitor of RNase to protect RNA in the course of the synthesis of complementary DNA
Peter Blackburn, Stanford Moore
openaire +2 more sources
Pancreatic Ribonuclease Distribution and Comparisons in Mammals
Nature New Biology, 1973PANCREATIC RNAase is absent or present in very small amounts in the pancreas of species such as man, cat, seal and rabbit1. Likewise no RNAase activity has been found in the pancreatic juice of dog by Marchis-Mouren et al.2 and in the juice of cat and rabbit by Berndt3.
G.W. Welling +4 more
openaire +4 more sources
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
Kinetic constants for the transesterification of eight dinucleoside phosphates CpX and UpX by bovine and turtle pancreatic ribonuclease were determined. Both ribonucleases have a preference for purine nucleotides at the position X. However, bovine ribonuclease, like other mammalian ribonucleases, prefers 6-amino bases at this site, while turtle ...
Hideo Katoh +6 more
openaire +4 more sources
Kinetic constants for the transesterification of eight dinucleoside phosphates CpX and UpX by bovine and turtle pancreatic ribonuclease were determined. Both ribonucleases have a preference for purine nucleotides at the position X. However, bovine ribonuclease, like other mammalian ribonucleases, prefers 6-amino bases at this site, while turtle ...
Hideo Katoh +6 more
openaire +4 more sources
A pancreatic ribonuclease active at pH 4.5.
International journal of peptide & protein research, 2009When a homogenate of beef pancreas prepared at neutral pH is assayed for RNase activities at pH 4.5 and at pH 7.5, the specific activity at the acid pH is more than half that at neutral pH.
J. Batholeyns, S. Moore, W. Stein
semanticscholar +1 more source