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Author Wilson, M.T.; Ranson, R.J.; Masiakowski, P.; Czarnecka, E.; Brunori, M.
Title (up) A kinetic study of the pH-dependent properties of the ferric undecapeptide of cytochrome c (microperoxidase) Type Journal Article
Year 1977 Publication European Journal of Biochemistry / FEBS Abbreviated Journal Eur J Biochem
Volume 77 Issue 1 Pages 193-199
Keywords Animals; Cyanides; *Cytochrome c Group/metabolism; Ferric Compounds; Horses; Hydrogen-Ion Concentration; Imidazoles; Kinetics; Mathematics; Myocardium/enzymology; *Oligopeptides/metabolism; *Peptide Fragments/metabolism; Protein Binding; Spectrophotometry; Temperature
Abstract The ferric form of the haem undecapeptide, derived from horse cytochrome c by peptic digestion, undergoes at least three pH-induced transitions with pK values of 3.4, 5.8 and 7.6. Temperature-jump experiments suggest that the first of these is due to the binding of a deprotonated imidazole group to the feric iron while the second and third arise from the binding of the two available amino groups present (the alpha-NH2 of valine and the epsilon-NH2 of lysine). Molecular models indicate that steric retraints on the peptide dictate that these amino groups may only coordinate to iron atoms via intermolecular bonds, thus leading to the polymerization of the peptide. Cyanide binding studies are in agreement with these conclusions and also yield a value of 3.6 X 10(6) M-1 s-1 for the intrinsic combination constant of CN- anion with the haem. A model is proposed which describes the pH-dependent properties of the ferric undecapeptide.
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Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0014-2956 ISBN Medium
Area Expedition Conference
Notes PMID:20304 Approved no
Call Number Equine Behaviour @ team @ Serial 3814
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Author Gill, J.
Title (up) A new method for continuous recording of motor activity in horses Type Journal Article
Year 1991 Publication Comparative Biochemistry and Physiology. A, Comparative Physiology Abbreviated Journal Comp Biochem Physiol A
Volume 99 Issue 3 Pages 333-341
Keywords Animals; Circadian Rhythm; Female; Horses/*physiology; Monitoring, Physiologic/instrumentation/*veterinary; *Motor Activity; Signal Processing, Computer-Assisted
Abstract 1. The use of an electronic recorder for the horse motor activity was described. 2. Examples of different types of motor activities are given in Figs 1-8. 3. The ultradian pattern of activity in all records was stressed. 4. The possibility of receiving of more physiological informations by this type of apparatus is discussed.
Address Department of Vertebrate Animal Physiology, University of Warsaw, Poland
Corporate Author Thesis
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Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0300-9629 ISBN Medium
Area Expedition Conference
Notes PMID:1678331 Approved no
Call Number refbase @ user @ Serial 1950
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Author Saigo, S.
Title (up) A transient spin-state change during alkaline isomerization of ferricytochrome c Type Journal Article
Year 1981 Publication Journal of Biochemistry Abbreviated Journal J Biochem (Tokyo)
Volume 89 Issue 6 Pages 1977-1980
Keywords Animals; *Cytochrome c Group; Horses; Hydrogen-Ion Concentration; Isomerism; Kinetics; Myocardium/enzymology; Oxidation-Reduction; Spectrophotometry
Abstract Kinetic difference spectra during the alkaline isomerization of ferricytochrome c were obtained by the pH-jump method in the range of 540 to 655 nm. The spectrum of the transient intermediate, which appears during the course of the isomerization, was reproduced from the spectra. The intermediate showed an intense absorption band at 600 nm, indicating that it is a high spin or mixed spin species. This is in contrast to the stable neutral and alkaline forms which are low spin species. The transient spin-state change during the isomerization was also observed upon rapid oxidation of ferrocytochrome c at alkaline pH.
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Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0021-924X ISBN Medium
Area Expedition Conference
Notes PMID:6270075 Approved no
Call Number Equine Behaviour @ team @ Serial 3808
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Author Matzke, S.M.; Oubre, J.L.; Caranto, G.R.; Gentry, M.K.; Galbicka, G.
Title (up) Behavioral and immunological effects of exogenous butyrylcholinesterase in rhesus monkeys Type Journal Article
Year 1999 Publication Pharmacology, Biochemistry, and Behavior Abbreviated Journal Pharmacol Biochem Behav
Volume 62 Issue 3 Pages 523-530
Keywords Animals; Antibody Formation/drug effects; Behavior, Animal/*drug effects; Butyrylcholinesterase/*immunology/pharmacokinetics/*pharmacology; Cognition/drug effects; Color Perception/drug effects; Conditioning, Operant/drug effects; Discrimination Learning/drug effects; Half-Life; Horses; Humans; Macaca mulatta; Male
Abstract Although conventional therapies prevent organophosphate (OP) lethality, laboratory animals exposed to such treatments typically display behavioral incapacitation. Pretreatment with purified exogenous human or equine serum butyrylcholinesterase (Eq-BuChE), conversely, has effectively prevented OP lethality in rats and rhesus monkeys, without producing the adverse side effects associated with conventional treatments. In monkeys, however, using a commercial preparation of Eq-BuChE has been reported to incapacitate responding. In the present study, repeated administration of commercially prepared Eq-BuChE had no systematic effect on behavior in rhesus monkeys as measured by a six-item serial probe recognition task, despite 7- to 18-fold increases in baseline BuChE levels in blood. Antibody production induced by the enzyme was slight after the first injection and more pronounced following the second injection. The lack of behavioral effects, the relatively long in vivo half-life, and the previously demonstrated efficacy of BuChE as a biological scavenger for highly toxic OPs make BuChE potentially more effective than current treatment regimens for OP toxicity.
Address Walter Reed Army Institute of Research, Washington, DC 20307-5100, USA
Corporate Author Thesis
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Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0091-3057 ISBN Medium
Area Expedition Conference
Notes PMID:10080246 Approved no
Call Number Equine Behaviour @ team @ Serial 4064
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Author Czerlinski, G.H.; Wagner, M.; Erickson, J.O.; Theorell, H.
Title (up) Chemical relaxation studies on the system liver alcohol dehydrogenase, NADH and imidazole Type Journal Article
Year 1975 Publication Acta Chemica Scandinavica. Series B: Organic Chemistry and Biochemistry Abbreviated Journal Acta Chem Scand B
Volume 29 Issue 8 Pages 797-810
Keywords Alcohol Oxidoreductases/*metabolism; Animals; Computers; Hydrogen-Ion Concentration; Imidazoles/*metabolism; Kinetics; Liver/enzymology/*metabolism; Mathematics; Models, Chemical; NAD/*metabolism; Time Factors
Abstract Several years ago, Theorell and Czerlinski conducted experiments on the system of horse liver alcohol dehydrogenase, reduced nicotinamide adenine dinucleotide and imidazole, using the first version of the temperature jump apparatus with detection of changes in fluorescence. These early experiments were repeated with improved instrumentation and confirmed the early experiments in general terms. However, the improved detection system allowed to measure a slight concentration dependence of the relaxation time of around 3 ms. Furthermore, the chemical relaxation time was smaller than the one determined earlier (by factor 2). The data were evaluated much more rigorously than before, allowing an appropriate interpretation of the results. The observed relaxation time is largely due to rate constants in an interconversion of ternary complexes, which are faster than three (of the four) dissociation rate constants, determined previously by Theorell and McKinley-McKee.1,2 This fact contributed to earlier difficulties of finding any concentration dependence. However, the binding of imidazole to the binary enzyme-coenzyme complex can be made to couple kinetically into the interconversion rate of the two ternary complexes. The observed signal derives largely from the ternary complex(es). A substantial fluorescence signal change is associated with the observed relaxation process, suggesting a relocation of the imidazole in reference to the nicotinamide moiety of the bound coenzyme. Nine models are considered with two types of coupling of pre-equilibria (none-all). Quantitative evaluations favor the model with two ternary complexes connected by an interconversion outside the four-step (bimolecular) cycle. The ternary complex outside the cycle has much higher fluorescence yield than the one inside. The interconversion equilibrium is near unity for imidazole. If it would be shifted very much to the side of the “dead-end” complex (as in isobutyramide?!), stimulating action could not take place.
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Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0302-4369 ISBN Medium
Area Expedition Conference
Notes PMID:882 Approved no
Call Number refbase @ user @ Serial 3887
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Author Gulotta, M.; Gilmanshin, R.; Buscher, T.C.; Callender, R.H.; Dyer, R.B.
Title (up) Core formation in apomyoglobin: probing the upper reaches of the folding energy landscape Type Journal Article
Year 2001 Publication Biochemistry Abbreviated Journal Biochemistry
Volume 40 Issue 17 Pages 5137-5143
Keywords Animals; Apoproteins/*chemistry; Computer Simulation; Horses; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Myoglobin/*chemistry; *Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence/instrumentation/methods; Thermodynamics; Tryptophan/chemistry
Abstract An acid-destabilized form of apomyoglobin, the so-called E state, consists of a set of heterogeneous structures that are all characterized by a stable hydrophobic core composed of 30-40 residues at the intersection of the A, G, and H helices of the protein, with little other secondary structure and no other tertiary structure. Relaxation kinetics studies were carried out to characterize the dynamics of core melting and formation in this protein. The unfolding and/or refolding response is induced by a laser-induced temperature jump between the folded and unfolded forms of E, and structural changes are monitored using the infrared amide I' absorbance at 1648-1651 cm(-1) that reports on the formation of solvent-protected, native-like helix in the core and by fluorescence emission changes from apomyoglobin's Trp14, a measure of burial of the indole group of this residue. The fluorescence kinetics data are monoexponential with a relaxation time of 14 micros. However, infrared kinetics data are best fit to a biexponential function with relaxation times of 14 and 59 micros. These relaxation times are very fast, close to the limits placed on folding reactions by diffusion. The 14 micros relaxation time is weakly temperature dependent and thus represents a pathway that is energetically downhill. The appearance of this relaxation time in both the fluorescence and infrared measurements indicates that this folding event proceeds by a concomitant formation of compact secondary and tertiary structures. The 59 micros relaxation time is much more strongly temperature dependent and has no fluorescence counterpart, indicating an activated process with a large energy barrier wherein nonspecific hydrophobic interactions between helix A and the G and H helices cause some helix burial but Trp14 remains solvent exposed. These results are best fit by a multiple-pathway kinetic model when U collapses to form the various folded core structures of E. Thus, the results suggest very robust dynamics for core formation involving multiple folding pathways and provide significant insight into the primary processes of protein folding.
Address Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA
Corporate Author Thesis
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Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0006-2960 ISBN Medium
Area Expedition Conference
Notes PMID:11318635 Approved no
Call Number Equine Behaviour @ team @ Serial 3789
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Author Andersson, P.; Kvassman, J.; Lindstrom, A.; Olden, B.; Pettersson, G.
Title (up) Effect of NADH on the pKa of zinc-bound water in liver alcohol dehydrogenase Type Journal Article
Year 1981 Publication European Journal of Biochemistry / FEBS Abbreviated Journal Eur J Biochem
Volume 113 Issue 3 Pages 425-433
Keywords Alcohol Oxidoreductases/*metabolism; Aldehydes/metabolism; Animals; Binding Sites; Cinnamates/metabolism; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Liver/*metabolism; NAD/*metabolism; Water/metabolism; Zinc/metabolism
Abstract Equilibrium constants for coenzyme binding to liver alcohol dehydrogenase have been determined over the pH range 10--12 by pH-jump stop-flow techniques. The binding of NADH or NAD+ requires the protonated form of an ionizing group (distinct from zinc-bound water) with a pKa of 10.4. Complex formation with NADH exhibits an additional dependence on the protonation state of an ionizing group with a pKa of 11.2. The binding of trans-N,N-dimethylaminocinnamaldehyde to the enzyme . NADH complex is prevented by ionization of the latter group. It is concluded from these results that the pKa-11.2-dependence of NADH binding most likely derives from ionization of the water molecule bound at the catalytic zinc ion of the enzyme subunit. The pKa value of 11.2 thus assigned to zinc-bound water in the enzyme . NADH complex appears to be typical for an aquo ligand in the inner-sphere ligand field provided by the zinc-binding amino acid residues in liver alcohol dehydrogenase. This means that the pKa of metal-bound water in zinc-containing enzymes can be assumed to correlate primarily with the number of negatively charged protein ligands coordinated by the active-site zinc ion.
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Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0014-2956 ISBN Medium
Area Expedition Conference
Notes PMID:7011796 Approved no
Call Number Equine Behaviour @ team @ Serial 3810
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Author Wilson, M.T.; Silvestrini, M.C.; Morpurgo, L.; Brunori, M.
Title (up) Electron transfer kinetics between Rhus vernicifera stellacyanin and cytochrome c (horse heart cytochrome c and Pseudomonas cytochrome c551) Type Journal Article
Year 1979 Publication Journal of Inorganic Biochemistry Abbreviated Journal J Inorg Biochem
Volume 11 Issue 2 Pages 95-100
Keywords Animals; Copper; Cytochrome c Group/*metabolism; Electron Transport; Kinetics; Metalloproteins/*metabolism; Plant Proteins/*metabolism; *Plants, Toxic; Pseudomonas aeruginosa/*metabolism; Toxicodendron/*metabolism
Abstract The electron transfer reactions between Rhus vernicifera stellacyanin and either horse heart cytochrome c or Pseudomonas aeruginosa cytochrome c551 were investigated by rapid reaction techniques. The time course of electron transfer is monophasic under all conditions, and thus consistent with a simple formulation of the reaction. Both stopped-flow and temperature-jump experiments yield equilibrium constants in reasonable agreement with values calculated from the redox potentials. The differences in reaction rate between the two cytochromes and stellacyanin are discussed in terms of the Marcus theory.
Address
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0162-0134 ISBN Medium
Area Expedition Conference
Notes PMID:228006 Approved no
Call Number refbase @ user @ Serial 3879
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Author Kordal, R.J.; Parsons, S.M.
Title (up) Liver alcohol dehydrogenase subunit equivalence studied by rapid sampling of alcohol product formed from sequentially bound [4α-3H]NADH Type Journal Article
Year 1979 Publication Archives of Biochemistry and Biophysics Abbreviated Journal
Volume 194 Issue 2 Pages 439-448
Keywords
Abstract Horse liver alcohol dehydrogenase has been claimed to exhibit presteady-state “half-of-the-sites” reactivity with aromatic substrates under some circumstances. To clarify the role of half-of-the-sites reactivity in liver alcohol dehydrogenase the direct sampling of the alcohol product formed immediately after initiation of the reaction was studied using a rapid sampling device and [4α-3H]NADH. Liver alcohol dehydrogenase which contained a very low mole-ratio of [4α-3H]NADH bound to one subunit of the dimer was rapidly mixed with excess 4-(2'-imidazolylazo)benzaldehyde substrate and nonradioactive NADH to initiate the reaction, which was allowed to proceed for a short time before it was quenched. If strong HClO4 quench was used isolation of total free and bound azoalcohol product was possible. If NaOH quench was used isolation only of the azoalcohol product released by the enzyme was possible since most enzyme-bound azoalcohol was reversed back to azoaldehyde by the base. The pH-jump reversal reaction also was characterized spectroscopically by stopped flow technique. Nearly fullsites reactivity was observed for reaction in either direction. Furthermore (4α-3H]NADH bound firstly to one subunit in the dimer reacted essentially identically to NADH bound secondly to the other subunit. Thus, half-of-the-sites reactivity was not observed in these experiments nor did they give any indication of liver alcohol dehydrogenase active site nonequivalence induced by coenzyme binding or reaction.
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Notes Approved no
Call Number refbase @ user @ Serial 3983
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Author Polverini, E.; Cugini, G.; Annoni, F.; Abbruzzetti, S.; Viappiani, C.; Gensch, T.
Title (up) Molten globule formation in apomyoglobin monitored by the fluorescent probe Nile Red Type Journal Article
Year 2006 Publication Biochemistry Abbreviated Journal Biochemistry
Volume 45 Issue 16 Pages 5111-5121
Keywords Animals; Apoproteins/*chemistry/*metabolism; Binding Sites; Computer Simulation; Fluorescent Dyes/analysis; Horses; Hydrogen-Ion Concentration; Models, Molecular; Myoglobin/*chemistry/*metabolism; Oxazines/*analysis/chemistry; Protein Binding; Protein Folding; Protein Structure, Tertiary
Abstract The interaction of nile red (NR) with apomyoglobin (ApoMb) in the native (pH 7) and molten globule (pH 4) states was investigated using experimental and computational methods. NR binds to hydrophobic locations in ApoMb with higher affinity (K(d) = 25 +/- 5 microM) in the native state than in the molten globule state (K(d) = 52 +/- 5 microM). In the molten globule state, NR is located in a more hydrophobic environment. The dye does not bind to the holoprotein, suggesting that the binding site is located at the heme pocket. In addition to monitoring steady-state properties, the fluorescence emission of NR is capable of tracking submillisecond, time-resolved structural rearrangements of the protein, induced by a nanosecond pH jump. Molecular dynamics simulations were run on ApoMb at neutral pH and at pH 4. The structure obtained for the molten globule state is consistent with the experimentally available structural data. The docking of NR with the crystal structure shows that the ligand binds into the binding pocket of the heme group, with an orientation bringing the planar ring system of NR to overlap with the position of two of the heme porphyrin rings in Mb. The docking of NR with the ApoMb structure at pH 4 shows that the dye binds to the heme pocket with a slightly less favorable binding energy, in keeping with the experimental K(d) value. Under these conditions, NR is positioned in a different orientation, reaching a more hydrophobic environment in agreement with the spectroscopic data.
Address Dipartimento di Fisica, Universita degli Studi di Parma, Viale G. P. Usberti 7/A, 43100 Parma, Italy
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0006-2960 ISBN Medium
Area Expedition Conference
Notes PMID:16618100 Approved no
Call Number Equine Behaviour @ team @ Serial 3763
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