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Results: 21 to 26 of 26

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Roles of the vinyl chloride oxidation products 1-chlorooxirane and 2-chloroacetaldehyde in the in vitro formation of etheno adducts of nucleic acid bases [corrected].
Guengerich FP
(1992) Chem Res Toxicol 5: 2-5
MeSH Terms: Acetaldehyde, Animals, Cytochrome P-450 Enzyme System, DNA, Ethylene Oxide, Horses, In Vitro Techniques, Kinetics, Male, Microsomes, Liver, Oxidation-Reduction, Rats, Rats, Inbred Strains, Vinyl Chloride
Added March 5, 2014
0 Communities
1 Members
0 Resources
14 MeSH Terms
A physiologic concept of exercise-induced pulmonary hemorrhage in horses.
Roberts LJ, Knight VA
(1992) J Am Vet Med Assoc 201: 666-7
MeSH Terms: Animals, Hemorrhage, Horse Diseases, Horses, Lung Diseases, Physical Exertion
Added December 10, 2013
0 Communities
1 Members
0 Resources
6 MeSH Terms
Disturbing GTP-binding protein function through microinjection into the visual cell of Limulus.
Stieve H, Niemeyer B, Aktories K, Hamm HE
(1992) Z Naturforsch C 47: 915-21
MeSH Terms: Animals, Antibodies, Monoclonal, Horseshoe Crabs, Kinetics, Light, Membrane Potentials, Microinjections, Photoreceptor Cells, Poly(ADP-ribose) Polymerases, Time Factors, Transducin, Visual Perception
Show Abstract · Added December 10, 2013
We have tested the action of three agents microinjected into the ventral nerve photoreceptor of Limulus on the electrical response to dim light. 1. A monoclonal antibody (mAb 4A) against the G alpha subunit of frog transducin reduces the size of the receptor current to 60%, suggesting an interaction with G alpha in the Limulus photoreceptor. 2. Injection of Clostridium botulinum ADP-ribosyltransferase C3 reduces the size to 46%; latency is not affected. The results imply that small GTP-binding proteins play a functional role in photoreception of invertebrates. 3. Injection of GDP-beta-S reduces dose-dependently the size of the receptor current to 15% and prolongs the latency to 200%, presumably by reducing number and rate of G-protein activations.
0 Communities
1 Members
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12 MeSH Terms
Chemical studies of erythrocyte membrane glycoproteins from several species.
Hudson BG, Wegener LJ, Wingate JM, Carraway KL
(1975) Comp Biochem Physiol B 51: 127-35
MeSH Terms: Acetylgalactosamine, Amino Acids, Animals, Cattle, Cell Membrane, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Erythrocytes, Fucose, Galactose, Glycoproteins, Hexosamines, Hexoses, Horses, Humans, Molecular Weight, Sheep, Sialic Acids, Sodium Dodecyl Sulfate
Added December 10, 2013
1 Communities
1 Members
0 Resources
19 MeSH Terms
Lactoperoxidase-catalyzed iodination of horse cytochrome c:monoiodotyrosyl 74 cytochrome c.
Osheroff N, Feinberg BA, Margoliash E, Morrison M
(1977) J Biol Chem 252: 7743-51
MeSH Terms: Animals, Circular Dichroism, Cytochrome c Group, Electron Transport, Horses, Lactoperoxidase, Monoiodotyrosine, Myocardium, Peptide Fragments, Peroxidases, Protein Conformation, Spectrophotometry, Ultraviolet, Tyrosine
Show Abstract · Added March 5, 2014
Iodination of horse cytochrome c with the lactoperoxidase-hydrogen peroxide-iodide system results initially in the formation of the monoiodotyrosyl 74 derivative. This singly modified protein was obtained in pure form by ion exchange chromatography and preparative column electrophoresis. It shows an intact 695 nm absorption band, the midpoint potential of the native protein, a nuclear magnetic resonance spectrum which indicates an undisturbed heme crevice structure, a normal reaction with antibodies directed against native horse cytochrome c, and circular dichroic spectra in which the only changes from those of the native protein can be ascribed to the spectral properties of iodotyrosine itself. This conformationally intact derivative reacts with the succinate-cytochrome c reductase and the cytochrome c oxidase systems of beef mitochondrial particle preparations indistinguishably from the unmodified protein, showing that the region including tyrosine 74 is not involved in these enzymic electron transfer functions of the protein. The circular dichroic spectra of this derivative indicate that the minima observed at 288 and 282 nm in the spectrum of native ferricytochrome c originate from tyrosyl residue 74.
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13 MeSH Terms
Site-specific anti-cytochrome c antibodies. Inhibition of the reactions between cytochrome c and its respiratory chain electron exchange partners.
Osheroff N, Jemmerson R, Speck SH, Ferguson-Miller S, Margoliash E
(1979) J Biol Chem 254: 12717-24
MeSH Terms: Animals, Antibodies, Antigen-Antibody Complex, Binding Sites, Antibody, Cytochrome c Group, Electron Transport, Epitopes, Horses, Immunoglobulin Fab Fragments, Kinetics, Models, Molecular, Protein Conformation, Rabbits
Added March 5, 2014
0 Communities
1 Members
0 Resources
13 MeSH Terms