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	Author	Dirikolu, L.; Lehner, A.F.; Karpiesiuk, W.; Hughes, C.; Woods, W.E.; Boyles, J.; Harkins, J.D.; Troppmann, A.; Tobin, T.
	Title	Detection, quantification, metabolism, and behavioral effects of selegiline in horses			Type	Journal Article
	Year	2003	Publication	Veterinary Therapeutics : Research in Applied Veterinary Medicine	Abbreviated Journal	Vet Ther
	Volume	4	Issue	3	Pages	257-268
	Keywords	Administration, Oral; Animals; Behavior, Animal/drug effects; Female; Horses/metabolism; Mass Spectrometry/veterinary; Monoamine Oxidase Inhibitors/administration & dosage/blood/pharmacokinetics/pharmacology/urine; Selegiline/administration & dosage/blood/*pharmacokinetics/pharmacology/urine; Substance Abuse Detection/veterinary
	Abstract	Selegiline ([R]-[-]N,alpha-dimethyl-N-2- propynylphenethylamine or l-deprenyl), an irreversible inhibitor of monoamine oxidase, is a classic antidyskinetic and antiparkinsonian agent widely used in human medicine both as monotherapy and as an adjunct to levodopa therapy. Selegiline is classified by the Association of Racing Commissioners International (ARCI) as a class 2 agent, and is considered to have high abuse potential in racing horses. A highly sensitive LC/MS/MS quantitative analytical method has been developed for selegiline and its potential metabolites amphetamine and methamphetamine using commercially available deuterated analogs of these compounds as internal standards. After administering 40 mg of selegiline orally to two horses, relatively low (<60 ng/ml) concentrations of parent selegiline, amphetamine, and methamphetamine were recovered in urine samples. However, relatively high urinary concentrations of another selegiline metabolite were found, tentatively identified as N- desmethylselegiline. This metabolite was synthesized and found to be indistinguishable from the new metabolite recovered from horse urine, thereby confirming the chemical identity of the equine metabolite. Additionally, analysis of urine samples from four horses dosed with 50 mg of selegiline confirmed that N-desmethylselegiline is the major urinary metabolite of selegiline in horses. In related behavior studies, p.o. and i.v. administration of 30 mg of selegiline produced no significant changes in either locomotor activities or heart rates.
	Address	Department of Biomedical Sciences, College of Veterinary Medicine, Nursing and Allied Health, Tuskegee University, Tuskegee, AL 36088, USA
	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	1528-3593	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:15136987			Approved	no
	Call Number				Serial	1901
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	Author	Sukhomlinov, B.F.; Korobov, V.N.; Gonchar, M.V.; Datsiuk, L.A.; Korzhev, V.A.
	Title	[Comparative analysis of the peroxidase activity of myoglobins in mammals]			Type	Journal Article
	Year	1987	Publication	Zhurnal Evoliutsionnoi Biokhimii i Fiziologii	Abbreviated Journal	Zh Evol Biokhim Fiziol
	Volume	23	Issue	1	Pages	37-41
	Keywords	Amino Acid Sequence; Animals; Ecology; Evolution; Kinetics; Mammals/metabolism; Myoglobin/metabolism; Peroxidases/metabolism
	Abstract	Studies have been made on the peroxidase activity of metmyoglobins in animals from various ecological groups--the horse Equus caballus, cattle Bos taurus, beaver Castor fiber, otter Lutra lutra, mink Mustela vison and dog Canis familiaris. It was found that the level of this activity in diving animals depends on the duration of their diving, whereas in terrestrial species--on the strength of muscular contraction.
	Address
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	Russian	Summary Language		Original Title	Sravnitel'nyi analiz peroksidaznoi aktivnosti mioglobinov u mlekopitaiushchikh
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0044-4529	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:3564776			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	2681
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	Author	Bykov, S.; Lednev, I.; Ianoul, A.; Mikhonin, A.; Munro, C.; Asher, S.A.
	Title	Steady-state and transient ultraviolet resonance Raman spectrometer for the 193-270 nm spectral region			Type	Journal Article
	Year	2005	Publication	Applied Spectroscopy	Abbreviated Journal	Appl Spectrosc
	Volume	59	Issue	12	Pages	1541-1552
	Keywords	Animals; Equipment Design; Equipment Failure Analysis; Horses; Kinetics; Metmyoglobin/analysis; Myocardium/metabolism; Reproducibility of Results; Sensitivity and Specificity; Spectrophotometry, Ultraviolet/instrumentation/methods; Spectrum Analysis, Raman/instrumentation/methods
	Abstract	We describe a state-of-the-art tunable ultraviolet (UV) Raman spectrometer for the 193-270 nm spectral region. This instrument allows for steady-state and transient UV Raman measurements. We utilize a 5 kHz Ti-sapphire continuously tunable laser (approximately 20 ns pulse width) between 193 nm and 240 nm for steady-state measurements. For transient Raman measurements we utilize one Coherent Infinity YAG laser to generate nanosecond infrared (IR) pump laser pulses to generate a temperature jump (T-jump) and a second Coherent Infinity YAG laser that is frequency tripled and Raman shifted into the deep UV (204 nm) for transient UV Raman excitation. Numerous other UV excitation frequencies can be utilized for selective excitation of chromophoric groups for transient Raman measurements. We constructed a subtractive dispersion double monochromator to minimize stray light. We utilize a new charge-coupled device (CCD) camera that responds efficiently to UV light, as opposed to the previous CCD and photodiode detectors, which required intensifiers for detecting UV light. For the T-jump measurements we use a second camera to simultaneously acquire the Raman spectra of the water stretching bands (2500-4000 cm(-1)) whose band-shape and frequency report the sample temperature.
	Address	Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA
	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	0003-7028	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:16390595			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3767
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	Author	Abbruzzetti, S.; Viappiani, C.; Sinibaldi, F.; Santucci, R.
	Title	Kinetics of histidine dissociation from the heme Fe(III) in N-fragment (residues 1-56) of cytochrome c			Type	Journal Article
	Year	2004	Publication	The Protein Journal	Abbreviated Journal	Protein J
	Volume	23	Issue	8	Pages	519-527
	Keywords	Animals; Cytochromes c/chemistry; Enzyme Activation; Histidine/chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Lasers; Ligands; Peptide Mapping; Photolysis; Spectrophotometry
	Abstract	We have here investigated the dissociation kinetics of the His side chains axially ligated to the heme-iron in the ferric (1-56 residues) N-fragment of horse cyt c. The ligand deligation induced by acidic pH-jump occurs as a biexponential process with different pre-exponential factors, consistent with a structural heterogeneity in solution and the presence of two differently coordinated species. In analogy with GuHCl-denatured cyt c, our data indicate the presence in solution of two ferric forms of the N-fragment characterized by bis-His coordination, as summarized in the following scheme: His18-Fe(III)-His26 <==> His18-Fe(III)-His33. We have found that the pre-exponential factors depend on the extent of the pH-jump. This may be correlated with the different pKa values shown by His26 and His33; due to steric factors, His26 binds to the heme-Fe(III) less strongly than His33, as recently shown by studies on denatured cyt c. Interestingly, the two lifetimes are affected by temperature but not by the extent of the pH-jump. The lower pKa for the deligation reaction required the use of an improved laser pH-jump setup, capable of inducing changes in H+ concentration as large as 1 mM after the end of the laser pulse. For the ferric N-fragment, close activation entropy values have been determined for the two histidines coordinated to the iron; this result significantly differs from that for GuHCl-denatured cyt c, where largely different values of activation entropy were calculated. This underlines the role played by the missing segment (residues 57-104) peptide chain in discriminating deligation of the “nonnative” His from the sixth coordination position of the metal.
	Address	Dipartimento di Fisica, Universita degli Studi di Parma, Parco Area delle Scienze 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	1572-3887	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:15648974			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3770
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	Author	Hirota, S.; Suzuki, M.; Watanabe, Y.
	Title	Hydrophobic effect of trityrosine on heme ligand exchange during folding of cytochrome c			Type	Journal Article
	Year	2004	Publication	Biochemical and Biophysical Research Communications	Abbreviated Journal	Biochem Biophys Res Commun
	Volume	314	Issue	2	Pages	452-458
	Keywords	Amino Acids/chemistry; Animals; Cytochromes c/chemistry; Heme/chemistry; Histidine/chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium/chemistry; Peptides/chemistry; Protein Folding; Spectrophotometry; Spectrum Analysis, Raman; Tyrosine/analogs & derivatives/chemistry
	Abstract	Effect of a hydrophobic peptide on folding of oxidized cytochrome c (cyt c) is studied with trityrosine. Folding of cyt c was initiated by pH jump from 2.3 (acid-unfolded) to 4.2 (folded). The Soret band of the 2-ms transient absorption spectrum during folding decreased its intensity and red-shifted from 397 to 400 nm by interaction with trityrosine, whereas tyrosinol caused no significant effect. The change in the transient absorption spectrum by interaction with trityrosine was similar to that obtained with 100 mM imidazole, which showed that the population of the intermediate His/His coordinated species increased during folding of cyt c by interaction with trityrosine. The absorption change was biphasic, the fast phase (82+/-9s(-1)) corresponding to the transition from the His/H(2)O to the His/Met coordinated species, whereas the slow phase (24+/-3s(-1)) from His/His to His/Met. By addition of trityrosine, the relative ratio of the slow phase increased, due to increase of the His/His species at the initial stage of folding. According to the resonance Raman spectra of cyt c, the high-spin 6-coordinate and low-spin 6-coordinate species were dominated at pH 2.3 and 4.2, respectively, and these species were not affected by addition of trityrosine. These results demonstrated that the His/His species increased by interaction with trityrosine at the initial stage of cyt c folding, whereas the heme coordination structure was not affected by trityrosine when the protein was completely unfolded or folded. Hydrophobic peptides thus may be useful to study the effects of hydrophobic interactions on protein folding.
	Address	Department of Physical Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, 607-8414 Kyoto, Japan. hirota@mb.kyoto-phu.ac.jp
	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	0006-291X	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:14733927			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3777
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	Author	Hoang, L.; Maity, H.; Krishna, M.M.G.; Lin, Y.; Englander, S.W.
	Title	Folding units govern the cytochrome c alkaline transition			Type	Journal Article
	Year	2003	Publication	Journal of Molecular Biology	Abbreviated Journal	J Mol Biol
	Volume	331	Issue	1	Pages	37-43
	Keywords	Animals; Cytochrome c Group/chemistry; Horses; Hydrogen/chemistry; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Protein Folding; Protein Structure, Tertiary; Spectrum Analysis; Titrimetry
	Abstract	The alkaline transition of cytochrome c is a model for protein structural switching in which the normal heme ligand is replaced by another group. Stopped flow data following a jump to high pH detect two slow kinetic phases, suggesting two rate-limiting structure changes. Results described here indicate that these events are controlled by the same structural unfolding reactions that account for the first two steps in the reversible unfolding pathway of cytochrome c. These and other results show that the cooperative folding-unfolding behavior of protein foldons can account for a variety of functional activities in addition to determining folding pathways.
	Address	Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA. lhoang@mail.upenn.edu
	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	0022-2836	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:12875834			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3781
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	Author	Haruta, N.; Kitagawa, T.
	Title	Time-resolved UV resonance Raman investigation of protein folding using a rapid mixer: characterization of kinetic folding intermediates of apomyoglobin			Type	Journal Article
	Year	2002	Publication	Biochemistry	Abbreviated Journal	Biochemistry
	Volume	41	Issue	21	Pages	6595-6604
	Keywords	Animals; Apoproteins/chemistry; Circular Dichroism; Holoenzymes/chemistry; Horses; Hydrochloric Acid/chemistry; Hydrogen-Ion Concentration; Imidazoles/chemistry; Kinetics; Models, Molecular; Myoglobin/chemistry; Peptide Fragments/chemistry; Protein Folding; Protein Structure, Secondary; Spectrum Analysis, Raman/methods; Tryptophan/*chemistry; Ultraviolet Rays; Whales
	Abstract	The 244-nm excited transient UV resonance Raman spectra are observed for the refolding intermediates of horse apomyoglobin (h-apoMb) with a newly constructed mixed flow cell system, and the results are interpreted on the basis of the spectra observed for the equilibrium acid unfolding of the same protein. The dead time of mixing, which was determined with the appearance of UV Raman bands of imidazolium upon mixing of imidazole with acid, was 150 micros under the flow rate that was adopted. The pH-jump experiments of h-apoMb from pH 2.2 to 5.6 conducted with this device demonstrated the presence of three folding intermediates. On the basis of the analysis of W3 and W7 bands of Trp7 and Trp14, the first intermediate, formed before 250 micros, involved incorporation of Trp14 into the alpha-helix from a random coil. The frequency shift of the W3 band of Trp14 observed for this process was reproduced with a model peptide of the A helix when it forms the alpha-helix. In the second intermediate, formed around 1 ms after the start of refolding, the surroundings of both Trp7 and Trp14 were significantly hydrophobic, suggesting the formation of the hydrophobic core. In the third intermediate appearing around 3 ms, the hydrophobicity was relaxed to the same level as that of the pH 4 equilibrium intermediate, which was investigated in detail with the stationary state technique. The change from the third intermediate to the native state needs more time than 40 ms, while the appearance of the native spectrum after the mixing of the same solutions was confirmed separately.
	Address	School of Mathematical and Physical Sciences, The Graduate University for Advanced Studies, Myodaiji, Okazaki 444-8585, Japan
	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:12022863			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3785
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	Author	Abbruzzetti, S.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W.
	Title	Kinetics of histidine deligation from the heme in GuHCl-unfolded Fe(III) cytochrome C studied by a laser-induced pH-jump technique			Type	Journal Article
	Year	2001	Publication	Journal of the American Chemical Society	Abbreviated Journal	J Am Chem Soc
	Volume	123	Issue	27	Pages	6649-6653
	Keywords	Animals; Bacterial Proteins; Cytochrome c Group/chemistry; Guanidine/chemistry; Heme/chemistry; Histidine/chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Lasers; Ligands; Protein Folding
	Abstract	We have developed an instrumental setup that uses transient absorption to monitor protein folding/unfolding processes following a laser-induced, ultrafast release of protons from o-nitrobenzaldehyde. The resulting increase in [H(+)], which can be more than 100 microM, is complete within a few nanoseconds. The increase in [H(+)] lowers the pH of the solution from neutrality to approximately 4 at the highest laser pulse energy used. Protein structural rearrangements can be followed by transient absorption, with kinetic monitoring over a broad time range (approximately 10 ns to 500 ms). Using this pH-jump/transient absorption technique, we have examined the dissociation kinetics of non-native axial heme ligands (either histidine His26 or His33) in GuHCl-unfolded Fe(III) cytochrome c (cyt c). Deligation of the non-native ligands following the acidic pH-jump occurs as a biexponential process with different pre-exponential factors. The pre-exponential factors markedly depend on the extent of the pH-jump, as expected from differences in the pK(a) values of His26 and His33. The two lifetimes were found to depend on temperature but were not functions of either the magnitude of the pH-jump or the pre-pulse pH of the solution. The activation energies of the deligation processes support the suggestion that GuHCl-unfolded cyt c structures with non-native histidine axial ligands represent kinetic traps in unfolding.
	Address	Dipartimento di Fisica, Universita di Parma, Istituto Nazionale per la Fisica della Materia, 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	0002-7863	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:11439052			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3788
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	Author	Gulotta, M.; Gilmanshin, R.; Buscher, T.C.; Callender, R.H.; Dyer, R.B.
	Title	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
	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:11318635			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3789
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	Author	Abbruzzetti, S.; Crema, E.; Masino, L.; Vecli, A.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W.
	Title	Fast events in protein folding: structural volume changes accompanying the early events in the N-->I transition of apomyoglobin induced by ultrafast pH jump			Type	Journal Article
	Year	2000	Publication	Biophysical Journal	Abbreviated Journal	Biophys J
	Volume	78	Issue	1	Pages	405-415
	Keywords	Animals; Apoproteins/chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Myoglobin/chemistry; Protein Conformation; Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence
	Abstract	Ultrafast, laser-induced pH jump with time-resolved photoacoustic detection has been used to investigate the early protonation steps leading to the formation of the compact acid intermediate (I) of apomyoglobin (ApoMb). When ApoMb is in its native state (N) at pH 7.0, rapid acidification induced by a laser pulse leads to two parallel protonation processes. One reaction can be attributed to the binding of protons to the imidazole rings of His24 and His119. Reaction with imidazole leads to an unusually large contraction of -82 +/- 3 ml/mol, an enthalpy change of 8 +/- 1 kcal/mol, and an apparent bimolecular rate constant of (0.77 +/- 0.03) x 10(10) M(-1) s(-1). Our experiments evidence a rate-limiting step for this process at high ApoMb concentrations, characterized by a value of (0. 60 +/- 0.07) x 10(6) s(-1). The second protonation reaction at pH 7. 0 can be attributed to neutralization of carboxylate groups and is accompanied by an apparent expansion of 3.4 +/- 0.2 ml/mol, occurring with an apparent bimolecular rate constant of (1.25 +/- 0.02) x 10(11) M(-1) s(-1), and a reaction enthalpy of about 2 kcal/mol. The activation energy for the processes associated with the protonation of His24 and His119 is 16.2 +/- 0.9 kcal/mol, whereas that for the neutralization of carboxylates is 9.2 +/- 0.9 kcal/mol. At pH 4.5 ApoMb is in a partially unfolded state (I) and rapid acidification experiments evidence only the process assigned to carboxylate protonation. The unusually large contraction and the high energetic barrier observed at pH 7.0 for the protonation of the His residues suggests that the formation of the compact acid intermediate involves a rate-limiting step after protonation.
	Address	Dipartimento di Fisica, Universita di Parma, 43100 Parma, Italia
	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	0006-3495	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:10620304			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3792
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