Results 11 to 20 of about 22,977 (294)

On the Preparation of Bovine Pancreatic Ribonuclease A

open access: hybridJournal of Biological Chemistry, 1963
Arthur M. Crestfield   +2 more
openalex   +4 more sources

Affinity Labeling of Pancreatic Ribonuclease

open access: hybridJournal of Biological Chemistry, 1971
Abstract Pyridoxal phosphate can be firmly bound by reduction with sodium borohydride to many enzymes in which it occurs. Such treatment has been used to label specifically parts of peptide chains in the vicinity of the bound coenzyme. Pyridoxal phosphate may form specific complexes with many proteins for which it has no known coenzyme function. Bovine
Gary E. Means, Robert E. Feeney
openalex   +4 more sources

Engineering and production of recombinant bovine pancreatic ribonuclease enzyme (RNase A) as a potential therapeutic [PDF]

open access: yesمجله بیوتکنولوژی کشاورزی, 2021
Objective  Immunotoxins are one of the most promising ways in therapeutic fields, specially cancer therapy which have a unique toxin-antibody structure, and kill the cancer cell by passing through the cell membrane and entering the target cell.
Masoume Vakili-Azghandi   +3 more
doaj   +1 more source

Horse Pancreatic Ribonuclease [PDF]

open access: yesEuropean Journal of Biochemistry, 1974
Horse ribonuclease was purified after acid extraction of pancreas by ammonium sulfate fractionation and chromatography on CM‐cellulose. It is a glycoprotein with an average molecular weight of about 18000. The pure enzyme was chromatographically and electrophoretically heterogeneous due to the heterogeneity of the carbohydrate moiety.The amino‐acid ...
A. J. Scheffer, Jaap J. Beintema
openaire   +4 more sources

MicroRNA drop in the bloodstream and microRNA boost in the tumour caused by treatment with ribonuclease A leads to an attenuation of tumour malignancy. [PDF]

open access: yesPLoS ONE, 2013
Novel data showing an important role of microRNAs in mediating tumour progression opened a new field of possible molecular targets for cytotoxic ribonucleases.
Nadezhda Mironova   +5 more
doaj   +1 more source

A novel circ_0099999/miR-330-5p/FSCN1 ceRNA crosstalk in pancreatic cancer

open access: yesAutoimmunity, 2021
Background Pancreatic cancer is a lethal malignancy in both sexes throughout the world. Circular RNAs (circRNAs) have been implicated in the development of pancreatic cancer by operating as competing endogenous RNAs (ceRNAs).
Yang Wang   +5 more
doaj   +1 more source

Histone deacetylase 2-mediated deacetylation of the Ribonuclease 1 promoter in inflamed human endothelial cells [PDF]

open access: yes, 2020
Endothelial cells (ECs) function as protective barrier to separate the blood from the surrounding tissue by conducting crucial roles in regulation and maintenance of vascular homeostasis, such as control of vessel permeability or coagulation.
Bedenbender, Katrin
core   +1 more source

Intramolecular interactions in pancreatic ribonucleases [PDF]

open access: yesProtein Science, 1992
AbstractA detailed analysis of the composition and properties of hydrophobic nuclei and microclusters in pancreatic ribonuclease A (RNase A) has been carried out. Distance calculations for all noncovalently bonded atoms revealed that the average number of nonpolar contacts between a side chain of an amino acid and its neighbors is substantially larger ...
Bangalore K. Sathyanarayana   +3 more
openaire   +3 more sources

A novel ligand-receptor relationship between families of ribonucleases and receptor tyrosine kinases

open access: yesJournal of Biomedical Science, 2018
Pancreatic ribonuclease is known to participate in host defense system against pathogens, such as parasites, bacteria, and virus, which results in innate immune response. Nevertheless, its potential impact to host cells remains unclear.
Ying-Nai Wang   +2 more
doaj   +1 more source

Protein disulfide-isomerase interacts with a substrate protein at all stages along its folding pathway [PDF]

open access: yes, 2014
In contrast to molecular chaperones that couple protein folding to ATP hydrolysis, protein disulfide-isomerase (PDI) catalyzes protein folding coupled to formation of disulfide bonds (oxidative folding).
A Jansens   +54 more
core   +3 more sources

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