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Integrated spatial morpho-transcriptomics predicts functional traits in pancreatic cancer. [PDF]
Gong D +6 more
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Gemcitabine resistance by CITED4 upregulation via the regulation of BIRC2 expression in pancreatic cancer. [PDF]
Jeong EJ +8 more
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Insights on the dynamic behavior of protein disulfide isomerase in the solution environment through the SAXS technique. [PDF]
Sanyasi C +6 more
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Total Synthesis of Bovine Pancreatic Ribonuclease A
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Semisynthetic studies on bovine pancreatic ribonuclease
International Journal of Peptide and Protein Research, 1984The 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.
C, Di Bello +3 more
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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.
E J, COULSON, H, STEVENS
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Journal of Experimental Zoology, 2000
Bovine seminal ribonuclease (BS-RNase) contains the MxM (noncovalent dimer) and M=M (free monomer) in constant ratio. The aim of this work was to evaluate the effect of BS-RNase, its monomer and dimer forms, and also various mutants of this enzyme on meiotic completion in cattle oocytes.
T, Slavík +3 more
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Bovine seminal ribonuclease (BS-RNase) contains the MxM (noncovalent dimer) and M=M (free monomer) in constant ratio. The aim of this work was to evaluate the effect of BS-RNase, its monomer and dimer forms, and also various mutants of this enzyme on meiotic completion in cattle oocytes.
T, Slavík +3 more
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Dinitrophenylation and inactivation of bovine pancreatic ribonuclease A
Archives of Biochemistry and Biophysics, 1965Abstract 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
C H, Hirs, M, Halmann, J H, Kycia
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Enhancement of Bovine Pancreatic Ribonuclease Activity by Mercaptoethanol
Science, 1978Incubation of ribonuclease with 0.1 M mercaptoethanol at p H 8.5 can increase the enzyme's hydrolytic activity toward cytidine 2′,3′-monophosphate (cyclic CMP) under standard assay conditions.
J B, Watkins, F W, Benz
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Tandemization Endows Bovine Pancreatic Ribonuclease with Cytotoxic Activity
Journal of Molecular Biology, 2006Due to their ability to degrade RNA, selected members of the bovine pancreatic ribonuclease A (RNase A) superfamily are potent cytotoxins. These cytotoxic ribonucleases enter the cytosol of target cells, where they degrade cellular RNA and cause cell death.
Franziska, Leich +3 more
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