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.
Identification of uroliths by infrared spectroscopy.
Australian veterinary journal    December 1, 1986   Volume 63, Issue 12 393-396 doi: 10.1111/j.1751-0813.1986.tb15915.x
Manning RA, Blaney BJ.Wet chemical tests have deficiencies when applied to mixtures containing silica, which are common in the uroliths of some domestic animals. Consequently, the applicability of an infrared spectroscopic method was tested on 104 uroliths obtained from cattle, sheep, goats, horses, pigs, dogs, a chicken and a rabbit during diagnostic investigations. The following components were satisfactorily identified: silica, calcium oxalate, calcium carbonate, calcium phosphate, magnesium ammonium phosphate, magnesium phosphate and urates. The infrared characteristics of these compounds and their mixtures are...
Spectrofluorimetric study of the bile salt micelle binding site of pig and horse colipases.
Biochimica et biophysica acta    November 7, 1986   Volume 874, Issue 1 54-60 doi: 10.1016/0167-4838(86)90101-9
Granon S.Pig and horse colipases contain three tyrosine residues. In addition, horse colipase possesses a tryptophan residue. Some of the tyrosine residues are involved in the association of colipase and a bile salt micelle. The present report demonstrates that the aromatic residues responsible for colipase fluorescence are in an aqueous environment. In the presence of bile salt micelles, changes in colipase fluorescence properties indicate that the intrinsic fluorophores are located in a more hydrophobic environment upon colipase-micelle complex formation. In addition, the fluorescence of an NBD group...
Triplet-singlet energy transfer in the complex of auramine O with horse liver alcohol dehydrogenase.
Biochemistry    May 20, 1986   Volume 25, Issue 10 2897-2904 doi: 10.1021/bi00358a024
Weers JG, Maki AH.Triplet-singlet energy transfer has been studied in the complex formed between auramine O (AO) and horse liver alcohol dehydrogenase with optically detected magnetic resonance (ODMR) spectroscopy. The results show that Trp-15 and Tyr residues transfer triplet energy mainly by a trivial process, whereas Trp-314 transfers triplet energy by a Förster process with two observed lifetimes at 77 K of 170 and 50 ms. The different Förster energy-transfer lifetimes are ascribed either to quenching of the two Trp-314 residues of the dimer by a single asymmetrically bound AO or to two distinct conformat...
Two-dimensional 1H NMR studies of cytochrome c: assignment of the N-terminal helix.
Biochemistry    March 11, 1986   Volume 25, Issue 5 1100-1106 doi: 10.1021/bi00353a024
Wand AJ, Englander SW.The 1H resonances of 11 sequential amino acids in the N-terminal helix of horse ferrocytochrome c were studied by two-dimensional nuclear magnetic resonance techniques. All the main-chain protons from Lys-5 through Ala-15 and many of the side-chain protons were assigned. J-Correlated spectroscopy (COSY) was used to distinguish protons on neighboring bonds and to recognize amino acid types. Nuclear Overhauser effect spectroscopy (NOESY) was used to define spatially contiguous protons and to determine amino acid sequence neighbors. The relayed coherence experiment (relay COSY) was used to resolv...
Selenium determination by Zeeman atomic absorption spectrophotometry.
Veterinary and human toxicology    February 1, 1986   Volume 28, Issue 1 12-13 
Edwards WC, Blackburn TA.No abstract available
Copper concentration in cornea, iris, normal, and cataractous lenses and intraocular fluids of vertebrates.
Current eye research    January 1, 1986   Volume 5, Issue 1 69-76 doi: 10.3109/02713688608995168
Cook CS, McGahan MC.A method using electrothermal atomic absorption spectroscopy was developed for the determination of copper (Cu) concentration in the cornea, iris, and lens of a variety of species, including dog, cat, rabbit, horse, and toad. Previously described methods were used to determine Cu in aqueous and vitreous humor. There was little difference between copper levels in the same tissue or fluid across the species. However, there were age and pathology-related changes in Cu concentration of the aqueous humor, cornea, and lens. In the groups of older dogs, the Cu concentration of the aqueous humor and c...
Identification of betamethasone and a major metabolite in equine urine.
Journal of pharmaceutical and biomedical analysis    January 1, 1986   Volume 4, Issue 3 327-331 doi: 10.1016/0731-7085(86)80054-1
Skrabalak DS, Henion JD.Betamethasone and its major unconjugated metabolite, 6-beta-hydroxybetamethasone, were detected in equine urine by thin-layer chromatography and characterized by micro-liquid chromatography/mass spectrometry (micro-LC/MS). Their structures were confirmed by a combination of infrared spectroscopy and nuclear magnetic resonance spectroscopy.
Complexities in the denaturation of horse metmyoglobin by guanidine hydrochloride.
The Journal of biological chemistry    September 5, 1985   Volume 260, Issue 19 10458-10460 
Ahmad F.The denaturation of horse metmyoglobin by guanidine hydrochloride was studied at pH 6.4 and 25 degrees C. Measurements of both the peptide circular dichroism and the absorbance in the Soret region suggest that the extent of renaturation strongly depends on the time interval during which the protein is exposed to concentrated solutions of the denaturant. From the equilibrium measurements of the absorption in the Soret region, it is concluded that the unfolding of metmyoglobin is complex. This is further supported by kinetic studies of denaturation which suggest the occurrence of the least four ...
Identification of metabolites of methylprednisolone in equine urine.
Steroids    August 1, 1985   Volume 46, Issue 2-3 755-765 doi: 10.1016/0039-128x(85)90055-8
Gallicano KD, Ng RM, Young LM.Methylprednisolone and three metabolites, 17,21-dihydroxy-6 alpha-methyl-1,4-pregnadiene-3,11,20-trione, 6 alpha-methyl-17,20 beta,21-trihydroxy-1,4-pregnadiene-3,11-dione, and 6 alpha-methyl-11 beta,17,20 beta,21-tetrahydroxy-1,4-pregnadien-3-one were detected in equine urine after intraarticular administration of methylprednisolone acetate. All four compounds were excreted both in the unconjugated form and as glucuronic acid conjugates. They were identified by comparing data obtained from analyses by high performance liquid chromatography, thin-layer chromatography, ultraviolet spectroscopy ...
Iron deposition in apoferritin. Evidence for the formation of a mixed valence binuclear iron complex.
The Journal of biological chemistry    March 10, 1985   Volume 260, Issue 5 2926-2929 
Chasteen ND, Antanaitis BC, Aisen P.A preliminary EPR investigation of iron accumulation in apoferritin has identified paramagnetic species generated during the early stage of iron deposition within the apoprotein shell. A featureless resonance at g' = 4.3, attributable to solitary high spin Fe3+ ions bound to the protein, is generated when Fe(II) is added to apoferritin at a level of 0.5 Fe/subunit (12 Fe/molecule) followed by air oxidation. This resonance accounts for 36% of the added iron. The remainder is EPR-silent and is probably present as oligomeric Fe3+ species. The intensity of the g' = 4.3 signal is reduced 3-fold upo...
The value of spectrofluorometry for the diagnosis of contagious equine metritis.
Zentralblatt fur Veterinarmedizin. Reihe B. Journal of veterinary medicine. Series B    February 1, 1985   Volume 32, Issue 2 77-84 doi: 10.1111/j.1439-0450.1985.tb01942.x
Brown BS, Hyde WA, Timoney PJ, Ward J, Hulse J, Patterson F.No abstract available
Fluorescence depolarization studies of melanosomal membranes from different sources.
Physiological chemistry and physics and medical NMR    January 1, 1985   Volume 17, Issue 4 365-370 
Cavatorta P, Crippa PR, Ito AS, Casali E, Ferrari MB, Masotti L.In the present paper we report a comparative study of physical properties and biochemical composition of isolated melanosomal membranes extracted from bovine eyes and from an equine spleen melanoma. Some biophysical characteristics of such membranes were obtained by steady-state and time resolved fluorescence spectroscopy using DPH as fluorescent probe. By these methods we have measured both static fluorescence polarization and fluorescence lifetimes and from the experimental data we have calculated the rotational correlation times by Perrin's equation. Since dynamic and static parameters, suc...
Cholesteryl sulfate: the major polar lipid of horse hoof.
Journal of lipid research    December 1, 1984   Volume 25, Issue 12 1320-1323 
Wertz PW, Downing DT.The lipids of horse hoof have been analyzed by quantitative thin-layer chromatography. The major components include cholesterol (37-40%), six groups of ceramides (10-15%), and cholesteryl sulfate (15-20%). Free fatty acids are abundant (15.8%) in the outer fully keratinized hoof, but are present at only low levels (3.1%) in the softer hyponychium. The material identified as cholesteryl sulfate was isolated by preparative thin-layer chromatography and characterized by a combination of chemical, chromatographic, and spectroscopic methods. The infrared spectrum of the isolated material had absorp...
Analysis of the high- and low-spin Soret bands of horse-heart metmyoglobin complexes.
Biopolymers    July 1, 1984   Volume 23, Issue 7 1147-1167 doi: 10.1002/bip.360230702
Anusiem AC, Kelleher M.No abstract available
Kinetic study of CO and O2 binding to horse heart myoglobin reconstituted with synthetic hemes lacking methyl and vinyl side chains.
Archives of biochemistry and biophysics    June 1, 1984   Volume 231, Issue 2 366-371 doi: 10.1016/0003-9861(84)90399-0
Chang CK, Ward B, Ebina S.Carbon monoxide- and oxygen-binding rates and affinities were measured for horse heart myoglobins reconstituted with synthetic hemes lacking peripheral methyl and vinyl groups. There is an apparent correlation between heme size and ligand specificity, i.e. larger m values (ratios of CO vs O2 association rates, l'/k') with smaller hemes. However, this correlation broke down with the most dealkylated heme. This is interpreted as resulting from protein conformational changes altering the steric crowdedness at the O2-binding site. Spectral properties and autoxidation rates also corroborate this vi...
Isolation, partial identification and quantitative determination of four guaiphenesin glucuronides in plasma and urine of the horse by high-performance liquid chromatography.
Journal of chromatography    April 24, 1984   Volume 288, Issue 2 423-429 doi: 10.1016/s0021-9673(01)93718-5
Ketelaars HC, Peters JG, Anzion RB, Van Ginneken CA.The isolation, partial identification and quantitative determination of four guaiphenesin glucuronides in plasma and urine of the horse is described. The identity of the glucuronides was checked by UV and fluorescence spectrophotometry, by NMR spectrometry and by mass spectrometry after permethylation. The applicability of the procedure to pharmacokinetic studies is demonstrated.
A distinct environment for iron (III) in the complex with horse spleen apoferritin observed by x-ray absorption spectroscopy.
The Journal of biological chemistry    December 10, 1983   Volume 258, Issue 23 14076-14079 
Sayers DE, Theil EC, Rennick FJ.Cell-specific variations in apoferritin structure correlate with variations in iron metabolism that suggest functional specificity of the protein shell. Using EPR spectroscopy, we previously showed that vanadyl binds to specific sites on apoferritin, and that VO2+ binding is reduced by Fe(II) and Fe(III) (the natural substrates) and by metals known to influence iron storage (Chasteen, N. D., and Theil, E. C. (1982) J. Biol. Chem. 257, 7672-7677). Such observations suggest that the metal-binding site is important to apoferritin function and may define a location where the influence of cell-spec...
Studies on prolactin: conformational comparison of human, equine, and porcine pituitary prolactins.
Archives of biochemistry and biophysics    December 1, 1983   Volume 227, Issue 2 618-625 doi: 10.1016/0003-9861(83)90491-5
Bewley TA, Li CH.The conformations of human, equine, and porcine pituitary prolactins, as evidenced by various optical properties, have been compared. The alpha-helix contents of all three proteins are essentially identical to each other (60 +/- 5%), as well as to prolactins isolated from other mammalian species. Direct absorption (zero and second-order), difference absorption, fluorescence emission, and circular dichroism spectra suggest that the majority of tyrosine and tryptophan side chains in these three proteins exist in very similar microenvironments within the folded forms of the hormones. Thus, the ge...
Proton nuclear magnetic resonance studies of histidines in horse carbonic anhydrase I.
Biochimica et biophysica acta    October 28, 1983   Volume 748, Issue 2 300-307 doi: 10.1016/0167-4838(83)90307-2
Forsman C, Jonsson BH, Lindskog S.The 250 MHz 1H-NMR spectrum of horse carbonic anhydrase I (or B) (carbonate hydro-lyase, EC 4.2.1.1) was measured as a function of pH under various conditions. Eight resonances corresponding to histidine C-2 protons and four resonances corresponding to histidine C-4 protons were identified and assigned to individual histidine residues in the enzyme molecule. Substantial similarities between horse and human carbonic anhydrases I were demonstrated. While the human enzyme has three titratable histidine residues in its active site, the horse enzyme has only two, His-67 in the human enzyme being re...
Identification of 3 beta-hydroxy-5,7-pregnadien-20-one and 3 beta-hydroxy-5,7-androstadien-17-one as endogenous steroids in the fetal horse gonad.
The Journal of endocrinology    October 1, 1983   Volume 99, Issue 1 87-92 doi: 10.1677/joe.0.0990087
Tait AD, Santikarn S, Allen WR.The 5,7-dienes, 3 beta-hydroxy-5,7-pregnadien-20-one and 3 beta-hydroxy-5,7-androstadien-17-one were extracted from fetal horse gonads and purified by solvent partition, thin-layer chromatography and high performance liquid chromatography. The isolated steroids were identified by comparison with the synthetic steroids using ultraviolet and mass spectroscopy and by gas chromatography-mass spectroscopy. The identification of these compounds as endogenous steroids, together with the data on their biosynthesis reported previously, support the proposal that in the fetal horse gonad there is a 5,7-d...
[Study of conformational changes in alcohol dehydrogenase during its interaction with silochrome adsorbent by the EPR spectroscopy method].
Biokhimiia (Moscow, Russia)    June 1, 1983   Volume 48, Issue 6 970-974 
Kharakhonycheva NV, Likhtenshteĭn GI, Shkileva EA, Adamenkova MD.The possible use of EPR spectroscopy (spin labelling) for the study of horse liver alcohol dehydrogenase with a silochrome adsorbent is discussed. The rotatory diffusion of nitroxyl labels chemically linked to the enzyme was studied with reference to the time of the enzyme incubation with the adsorbent and the degree of its accumulation on the adsorbent surface. The mobility of nitroxyl radicals attached to the protein globules was shown to increase with time. It was concluded that the conformation of the enzyme molecules changes during their interaction with the adsorbent.
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