Analyze Diet

Topic:Spectroscopy

Spectroscopy is an analytical technique used to measure the interaction between matter and electromagnetic radiation. In equine research, spectroscopy is applied to assess various biological and chemical properties of horses. Techniques such as infrared spectroscopy, nuclear magnetic resonance (NMR) spectroscopy, and mass spectrometry are utilized to analyze tissues, fluids, and other biological samples. These methods provide insights into metabolic processes, nutritional status, and disease states in horses. Spectroscopy aids in the identification and quantification of biomolecules, contributing to the understanding of equine physiology and pathology. This page compiles peer-reviewed research studies and scholarly articles that explore the application, methodology, and findings of spectroscopic techniques in equine science.
Dansylarginine N-(3-ethyl-1.5-pentanediyl)amide. A potent and selective fluorescent inhibitor of butyrylcholinesterase.
Biochemical pharmacology    February 15, 1983   Volume 32, Issue 4 699-706 doi: 10.1016/0006-2952(83)90495-1
Brimijoin S, Mintz KP, Prendergast FG.Interactions between dansylarginine N-(3-ethyl-1,5-pentanediyl)amide (DAPA) and the cholinesterases were examined by the techniques of enzyme kinetics and fluorescence spectroscopy. When tested with partially purified enzyme preparations, DAPA was a potent inhibitor of butyrylcholinesterase (IC50 = 2 x 10(-7) M) but not of acetylcholinesterase (IC50 = 4 x 10(-4) M). For a detailed study of the effects of DAPA on butyrylcholinesterase (BuChE), the enzyme was purified to homogeneity from horse serum, with the aid of affinity chromatography on N-methyl acridinium. The kinetics of the inhibition o...
Further study of the chemical structure of the equine erythrocyte hematoside containing O-acetyl ester.
The Journal of biological chemistry    January 25, 1983   Volume 258, Issue 2 876-881 
Gasa S, Makita A, Kinoshita Y.The chemical structure of an equine hematoside, which contained an ester group and comprised 72% of the total erythrocyte gangliosides, was determined by means of nondestructive and destructive procedures. A 400-MHz nuclear magnetic resonance spectrum of the ganglioside in perdeuterodimethyl sulfoxide demonstrated three protons due to a methyl group of an acetyl moiety, as well as amide and anomeric protons which were compatible with those of the ordinary hematoside. The spin decoupling difference spectroscopy of the ganglioside revealed the presence of the following structures. [formula: see ...
The uptake of mepacrine by horse polymorphonuclear leucocytes in vitro.
The Journal of pharmacy and pharmacology    November 1, 1982   Volume 34, Issue 11 711-714 doi: 10.1111/j.2042-7158.1982.tb06205.x
Read NG, Trist DG.The uptake of mepacrine by isolated horse polymorphonuclear leucocytes (PMN) was measured using spectrophotofluorimetry. Two phases of uptake were observed, the first, rapid fraction, essentially complete by 10 min, and a second, slow fraction, which was still proceeding after 60 min. The appearance of mepacrine within the PMN was also visualized by fluorescence microscopy. Discrete yellow points of fluorescence were observed in the cytoplasm of PMN within 30 s. These discrete points corresponded both in size and number to the PMN granules. After 5 min, the nuclei showed faint fluorescence whi...
Iron binding by horse spleen apoferritin. A vanadyl(IV) EPR spin probe study.
The Journal of biological chemistry    July 10, 1982   Volume 257, Issue 13 7672-7677 
Chasteen ND, Theil EC.No abstract available
Resonance-enhanced Raman identification of a ternary chemical intermediate during the equine liver alcohol dehydrogenase reduction of p-(dimethylamino)benzaldehyde.
Biochemistry    April 27, 1982   Volume 21, Issue 9 2193-2202 doi: 10.1021/bi00538a031
Jagodzinski PW, Funk GF, Peticolas WL.The nature of the binding of aromatic aldehyde and aromatic alcohol substrates to the catalytic zinc of equine liver alcohol dehydrogenase has been studied by using resonance-enhanced Raman spectroscopy. When an excess of both enzyme and coenzyme to substrate is used, a stable ternary chemical intermediate is formed between liver alcohol dehydrogenase and the reduced coenzyme, nicotinamide adenine dinucleotide, and the aldehyde, p-(dimethylamino)benzaldehyde, in the pH range 8.5-0.6. Resonance-enhanced Raman spectra clearly show that this same intermediate is formed between the excess enzyme, ...
Bio-elemental analysis of horse dorsum hair with an energy dispersive x-ray microanalyzer.
Nihon juigaku zasshi. The Japanese journal of veterinary science    April 1, 1982   Volume 44, Issue 2 369-373 doi: 10.1292/jvms1939.44.369
Sato H, Yoshino M, Miyasaka S, Seta S, Uehara N, Mochizuki K.No abstract available
Limited trypsinolysis of porcine and equine colipases. Spectroscopic and kinetic studies.
Biochimica et biophysica acta    December 29, 1981   Volume 671, Issue 2 155-163 doi: 10.1016/0005-2795(81)90129-x
Rathelot J, Canioni P, Bosc-Bierne I, Sarda L, Kamoun A, Kaptein R, Cozzone PJ.Porcine and equine colipases have been submitted to mild tryptic digestion. Proteolysis occurs at the Arg5-Gly6 bond with the loss of the N-terminal pentapeptide. Studies of native and trypsin-treated colipases by circular dichroism and laser chemically induced dynamic nuclear polarization indicate that proteolysis induces conformational changes in the region of the tyrosine cluster. Experiments in the presence of phospholipid provide further evidence showing that these residues are in or close to the region of the protein interacting with aggregated lipids. Kinetic studies of the reaction of ...
Circular dichroism study of horse colipase interaction with bile salt.
Biochimica et biophysica acta    October 28, 1981   Volume 670, Issue 3 305-311 doi: 10.1016/0005-2795(81)90101-x
Canioni P, Julien R, Romanetti R, Cozzone P, Sarda L.No abstract available
Analysis of the potentiometric titration of reduced horse heart cytochrome c.
Biopolymers    October 1, 1981   Volume 20, Issue 10 2243-2252 doi: 10.1002/bip.1981.360201016
Marini MA, Martin CJ, Forlani L.No abstract available
Effects of dilution rates, animal species and instruments on the spectrophotometric determination of sperm counts.
Revue canadienne de biologie    June 1, 1981   Volume 40, Issue 2 173-180 
Rondeau M, Rouleau M.Using semen from bull, boar and stallion as well as different spectrophotometers, we established the calibration curves relating the optical density of a sperm sample to the sperm count obtained on the hemacytometer. The results show that, for a given spectrophotometer, the calibration curve is not characteristic of the animal species we studied. The differences in size of the spermatozoa are probably too small to account for the anticipated specificity of the calibration curve. Furthermore, the fact that different dilution rates must be used, because of the vastly different concentrations of ...
Rapid-scanning spectral evidence for catalytically nonequivalent but interconvertible forms of equine liver alcohol dehydrogenase.
Biochimie    February 1, 1981   Volume 63, Issue 2 97-102 doi: 10.1016/s0300-9084(81)80171-x
Koerber SC, Dunn MF.These rapid-scanning stopped-flow kinetic studies of the equine liver alcohol dehydrogenase-catalyzed reduction of p-nitrobenzaldehyde by NADH and (4R)-4-deuterio NADH (NADD) under single turnover conditions establish : (1) The reaction is biphasic using NADD as coenzyme, k1 approximately 200 sec-1, k2 = 0.5 sec-1 and the amplitude ratio (A1)/(A1 + A2) approximately equal to 0.5. (2) Each phase of the reaction involves the oxidation of enzyme-bound reduced coenzyme. (3) The recycling of sites in the presence of 20 mM pyrazole is negligible. (4) The rates of E(NAD-pyrazole) complex formation at...
Predicted secondary structure of horse muscle acylphosphatase. Comparison with circular dichroism measurements.
Physiological chemistry and physics    January 1, 1981   Volume 13, Issue 3 267-273 
Camici G, Manao G, Cappugi G, Ramponi G.We have predicted the secondary structure of horse muscle acylphosphatase by the statistical method of Chou and Fasman. In addition, we have studied the circular dichroism spectra of the enzyme, obtaining values for comparison to the predicted results. Discrepancies were found for the alpha-helix content estimated by the two methods.
The major metabolite of fentanyl in the horse.
Drug metabolism and disposition: the biological fate of chemicals    November 1, 1980   Volume 8, Issue 6 425-427 
Frincke JM, Henderson GL.Fentanyl, a potent, synthetic narcotic analgesic, has reportedly been used to "dope" racehorses. Urine was collected from a horse dosed with 70 mg of [3H]fentanyl, and the primary metabolite, a water-soluble, amphoteric compound, was isolated by high-pressure liquid chromatography and identified by spectroscopic analysis. This metabolite was found to be N-[1-(2-phenethyl-4-piperidinyl)] malonanilinic acid.
Involvement of lysines-72 and -79 in the alkaline isomerization of horse heart ferricytochrome c.
Biochemistry    March 18, 1980   Volume 19, Issue 6 1117-1120 doi: 10.1021/bi00547a012
Smith HT, Millett F.Spectrophotometric titrations of five singly modified horse heart ferricytochromes c, specifically (trifluoromethyl)phenylcarbamylated (CF3PhNHCO-) or trifluoroacetylated (CF3CO-) at lysines-13, -72, and -79, were carried out. The CF3PhNHCO-Lys-13, Lys-79, and CF3CO-Lys-79 derivatives all underwent alkaline isomerization with loss of the 695-nm band to low-spin species with an apparent pK of about 8.9, as did the unmodified cytochrome. However, modification of lysine-72 appeared to alter the reaction pathway since the CF3PhNHCO-Lys-72 derivative isomerized to a high-spin form with an apparent ...
Oxidation of (horse) hemoglobin by copper: an intermediate detected by electron spin resonance.
Biochemistry    September 4, 1979   Volume 18, Issue 18 3860-3865 doi: 10.1021/bi00585a005
Rifkind JM.The oxidation of horse hemoglobin by Cu(II) has been followed by the changes in the electron spin resonance spectra of copper. By stopped-flow and freeze-quenching techniques, it is shown that the second-order rate constant for the binding of Cu(II) to hemoglobin is greater than 5 X 10(5) mol-1 s-1 and the apparent first-order rate for the reduction of Cu(II) to Cu(I) is 0.051 s-1. It is also shown that the binding of Cu(II) to hemoglobin is followed by an alteration of the Cu(II) spectrum, decreasing the g values. This process has an apparent rate constant of 17 s-1 and presumably involves a ...
Sound spectography in the diagnosis of equine respiratory disorders: a preliminary report.
New Zealand veterinary journal    July 1, 1979   Volume 27, Issue 7 145-146 doi: 10.1080/00480169.1979.34629
Barnes GR, Brennan M, Goulden BE, Kirkland J.One problem in the diagnosis of subclinical roarers is that abnormal auditory signals occur only during a fast gait, and these fade quickly. This paper offers a novel technique to assist this problem. Sound recordings were obtained from five horses following exercise; two roarers, two non-roarers, and one suspected roarer. These signals were converted into spectrograms by Rayspan processing. All frequencies in the 0 to 2.25 kHz range during both inspiration and expiration, as well as occasional noises in the 2–4 kHz band, characterised roarers. Signals from non-roarers consisted of frequenci...
The effect of binding ions on the oxidation of horse heart ferrocytochrome c.
Canadian journal of biochemistry    May 1, 1979   Volume 57, Issue 5 372-377 doi: 10.1139/o79-047
Peterman BF, Morton RA.The research explores how different binding ions affect the oxidation speed of horse heart ferrocytochrome c, a protein, by potassium ferricyanide at a constant ionic strength. Studying the Ion Effect […]
Alkaline isomerization of horse and yeast cytochromes C. Spectrophotometric and circular dichroism studies.
International journal of peptide and protein research    November 1, 1978   Volume 12, Issue 5 233-236 
Looze Y, Polastro E, Deconinck M, Leonis J.Spectrophotometric studies of the alkaline isomerization of horse heart and yeast cytochrome c show that the haemoproteins from Saccharomyces cerevisiae differ significantly from the mammalian cytochrome c. Apparent pKa values of 8.41, 8.40 and 8.73 for isol-1-(the methylated and unmethylated forms) and iso-2-cytochrome c respectively, from baker's yeast were determined and compared with the value of 9.40 found for horse heart cytochrome c. The transitions, measured by observing the decrease of the absorbance at 695 nm as the pH increases, have been found to strictly parallel the decrease in a...
Fourier transform infrared spectroscopic study of molecular interactions in hemoglobin.
Applied optics    September 15, 1978   Volume 17, Issue 18 2985-2990 doi: 10.1364/AO.17.002985
Alben JO, Bare GH.Infrared absorption spectra of the alpha-104 (G11) cysteine SH group have been observed for aqueous solutions of hemoglobin derivatives from humans, pigs, and horses. The center frequencies ((nu)SH) show ligand sensitive patterns that are similar for the three species, with (nu)SH (HbCO) <(nu)SH (HbO(2) ~ HbCN) < (nu)SH (Hb(+)) <<(nu)SH (deoxyHb) for human and pig hemoglobins. The alpha-104 SH group is most strongly H-bonded (smallest (nu)SH), has the greatest range of (nu)SH (Hb ? HbCO) in human hemoglobin, and is least strongly H-bonded and has the smallest range of (nu)SH (Hb ? HbCO) in hor...
The presence of two (Na+ + K+)-ATPase inhibitors in equine muscle ATP: vanadate nad a dithioerythritol-dependent inhibitor.
Biochimica et biophysica acta    August 4, 1978   Volume 511, Issue 2 202-212 doi: 10.1016/0005-2736(78)90314-0
Quist EE, Hokin LE.A potent inhibitor of (Na+ + K+)-ATPase activity was purified from Sigma equine muscle ATP by cation- and anion-exchange chromatography. The isolated inhibitor was identified by atomic absorption spectroscopy and proton resonance spectroscopy to be an inorganic vanadate. The isolated vanadate and a solution of V2O5 inhibit sarcolemma (Na+ + K+)-ATPase with an I50 of 1 micrometer in the presence of 1 mM ethyleneglycol-bis-(beta-aminoethylether)-N,N'-tetraacetic acid (EGTA), 145 mM NaCl, 6mM MgCl2, 15 mM KCl and 2 mM synthetic ATP. The potency of the isolated vanadate is increased by free Mg2+. ...
Circular dichroic properties and conformation of thionicotinamide dinucleotides bound to horse-liver alcohol dehydrogenase.
European journal of biochemistry    February 1, 1978   Volume 83, Issue 2 593-599 doi: 10.1111/j.1432-1033.1978.tb12128.x
Joppich-Kuhn R, Luisi PL.The interaction between horse liver alcohol dehydrogenase and the oxidized and reduced forms of the 3-thionicotinamide--adenine dinucleotide coenzyme analogues (sNAD and sNADH) has been investigated by ultraviolet absorption, fluorescence and circular dichroism. The fluorescence of sNADH is enhanced when bound to the enzyme, and the protein fluorescence is quenched by both sNADH (60--65%) and sNAD (65%). The possible origin of the larger quenching produced by sNAD with respect to that of NAD is discussed. Coenzyme dissociation constants have been determined by monitoring the quenching of the p...
Physicochemical and biological characterizations of pregnant mare serum gonadotropin and its subunits.
Biochimica et biophysica acta    January 25, 1978   Volume 532, Issue 1 185-194 doi: 10.1016/0005-2795(78)90462-2
Papkoff H, Bewley TA, Ramachandran J.Pregnant mare serum gonadotropin and its subunits have been further characterized. Ultracentrifugation of the gonadotropin at pH 1.3 and 11.5 showed little evidence of dissociation compared to pH 8.2. Highly purified subunits are obtained by urea dissociation and ion-exchange chromatography followed by gel-filtration. Circular dichroism spectra of the gonadotropin and its subunits are much like those of ovine lutropin and its subunits in that there is little evidence for secondary structure and one or more tyrosine residues are inaccessible in the intact gonadotropin compared to the subunits. ...
Stability of horse muscle acylphosphatase to heat and to urea.
Physiological chemistry and physics    January 1, 1978   Volume 10, Issue 2 153-162 
Berti A, Stefani M, Camici G, Manao G, Ramponi G.The thermal stability of horse muscle acylphosphatase was investigated by measuring the inactivation constants at various pH and temperature values, and by differential spectra technique. This enzyme has high thermal stability in an acidic environment but is inactivated in an alkaline medium. It was found that the enzyme can be protected against such inactivation at pH 8.0 by increasing its concentration and the ionic strength of the solution. The effect of high urea concentrations on stability was also measured. It was found that spectral changes at 230 nm are related to urea inactivation of ...
Synthetic antigens. Horse “natural” antibodies against interpolymer of styrene and maleic acid (PSM).
Archivum immunologiae et therapiae experimentalis    January 1, 1978   Volume 26, Issue 1-6 67-71 
Ugorski M, Mikulska J, Skibiński G, Wieczorek Z, Lisowski J.Properties of horse natural anti-PSM antibodies are described. The antibodies were of IgG class. Electrostatic forces were mainly involved in reaction of PSM with horse antibodies. The reaction was inhibited by low molecular compounds resembling structural unit of PSM. Studies of difference spectra and ORD and CD spectra showed no major conformational changes in horse antibodies after reaction with PSM.
Comparative studies on blood serum alpha-L-fucosidases from several mammalian species.
Comparative biochemistry and physiology. B, Comparative biochemistry    January 1, 1978   Volume 60, Issue 4 459-461 doi: 10.1016/0305-0491(78)90077-9
Villar E, Calvo P, Cabezas JA.1. Peripheral blood serum alpha-L-fucosidases have been studied from various mammalian species: Sus scropha var domestica L. (pig), Capra hircus L. (goat), Bos taurus L. (bull, races Morucha and Charolais), Equus caballus L. (horse) and Equus asinus L. (donkey). 2. Fluorimetric and spectrophotometric procedures were used for determination of alpha-L-fucosidases. 3. alpha-L-Fucosidases were more active towards fluorescent substrates than towards chromogenic substrates. 4. pH optima values of the enzymes are: (A) 5.5 for sera from all above-mentioned species when fluorescent substrates were empl...
Lactoperoxidase-catalyzed iodination of horse cytochrome c:monoiodotyrosyl 74 cytochrome c.
The Journal of biological chemistry    November 10, 1977   Volume 252, Issue 21 7743-7751 
Osheroff N, Feinberg BA, Margoliash E, Morrison M.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 cha...
Circular dichroism of porcine, bovine, and equine pancreatic phospholipases A2 and their zymogens. Unusual conformations simulating helix content.
Biochimica et biophysica acta    October 26, 1977   Volume 494, Issue 2 285-292 doi: 10.1016/0005-2795(77)90157-x
Jirgensons B, de Haas GH.Conformation of porcine, bovine, and equine pancreatic phospholipases A2 (EC 3.1.1.4) and their zymogens was studied by the circular dichroism (CD) probe in the far and near ultraviolet spectral zones. All these phospholipases and their zymogens displayed CD curves suggesting the presence of moderate amounts of α-helical conformation. However, on the basis of known primary structure and recent X-ray structural analysis of prophospholipase A2 crystals (Drenth, J., Enzing, C.M., Kalk, K.H. and Vessies, J.C.A. (1976) Nature 264, 373–377), it has to be concluded that the positive CD band cen...
The structure of horse methaemoglobin at 2-0 A resolution.
Journal of molecular biology    August 15, 1977   Volume 114, Issue 3 385-414 doi: 10.1016/0022-2836(77)90256-x
Ladner RC, Heidner EJ, Perutz MF.No abstract available
Probing DNA quaternary ordering with circular dichroism spectroscopy: studies of equine sperm chromosomal fibers.
Biopolymers    March 1, 1977   Volume 16, Issue 3 573-582 doi: 10.1002/bip.1977.360160308
Sipski ML, Wagner TE.No abstract available
Rapid heterolysis of indophenyl acetate by a constituent of a preparation of horse serum cholinesterase.
Enzyme    January 1, 1977   Volume 22, Issue 2 130-136 doi: 10.1159/000458777
Hubbard CD, Shoupe TS.A transient phase for the hydrolysis of indophenyl acetate by the commercial preparation of horse serum cholinesterase was observed on a stopped-flow spectrophotometer. It was found that the transient process is a reaction of the ester with a major component of the preparation and is not caused by the serum cholinesterase enzyme. This noncholinesterase component was isolated and the dependence of its concentration and that of the ester upon the transient liberation of the indophenolate ion were determined. Studies with the isolated component and subsequent analyses have led to the tentative id...