Results 201 to 210 of about 23,635 (226)
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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.
BEINTEMA, JJ +4 more
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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
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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
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Human pancreatic ribonuclease presents higher endonucleolytic activity than ribonuclease A
Archives of Biochemistry and Biophysics, 2008Analyzing the pattern of oligonucleotide formation induced by HP-RNase cleavage shows that the enzyme does not act randomly and follows a more endonucleolytic pattern when compared to RNase A. The enzyme prefers the binding and cleavage of longer substrate molecules, especially when the phosphodiester bond that is broken is 8-11 nucleotides away from ...
M, Rodríguez +5 more
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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
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European Journal of Biochemistry, 1997
Mammalian ribonucleases constitute one of the fastest evolving protein families in nature. The addition of a four‐residue carboxyl‐terminal tail: Glu‐Asp‐Ser‐Thr (EDST) in human pancreatic ribonuclease (HPR) in comparison with bovine pancreatic RNase (RNase A) could have adaptive significance in humans.
H P, Bal, J K, Batra
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Mammalian ribonucleases constitute one of the fastest evolving protein families in nature. The addition of a four‐residue carboxyl‐terminal tail: Glu‐Asp‐Ser‐Thr (EDST) in human pancreatic ribonuclease (HPR) in comparison with bovine pancreatic RNase (RNase A) could have adaptive significance in humans.
H P, Bal, J K, Batra
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Newly observed binding mode in pancreatic ribonuclease
Journal of Molecular Biology, 1992Dinucleotides containing guanine, when soaked into crystals of bovine pancreatic ribonuclease, have been found to bind in an unexpected manner, quite unlike interpretations of earlier X-ray diffraction studies. This finding has prompted a reexamination of three mononucleotide-RNase complexes from this laboratory resulting in a re-interpretation of the ...
C F, Aguilar +4 more
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Biosynthesis of pancreatic ribonuclease
2012Methods have been developed for the study of amino acid incorporation into a specific protein under established conditions of net synthesis. The results of these studies have been reported and discussed. Synthesis and storage of the secretory proteins of mouse pancreas have been shown to occur between fifteen to twenty-one hours after pilocarpine ...
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24 Bovine Pancreatic Ribonuclease
1971Publisher Summary This chapter discusses the process of isolation, chromatography, structure, and molecular and catalytic properties of bovine pancreatic ribonuclease. At present there are three simple and widely used chromatographic procedures: (1) Hirs base their method on the carboxyl ion exchange resin IRC-50 with 0.2 M phosphate buffer pH 6.45 ...
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Research on Pancreatic Ribonuclease
The Journal of Biochemistry, 1961TYUNOSIN UKITA +2 more
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Ribonuclease Activity of Pancreatic Extracts
New England Journal of Medicine, 1977W A, Gahl, P J, Chesney, H C, Pitot
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