| Records |
| Author |
Traversa, D.; Otranto, D.; Iorio, R.; Giangaspero, A. |
| Title |
Molecular characterization of Thelazia lacrymalis (Nematoda, Spirurida) affecting equids: a tool for vector identification |
Type |
Journal Article |
| Year |
2005 |
Publication |
Molecular and Cellular Probes |
Abbreviated Journal |
Mol Cell Probes |
Volume  |
19 |
Issue |
4 |
Pages |
245-249 |
| Keywords |
Animals; Horse Diseases/parasitology; Horses/*parasitology; Insect Vectors/*parasitology; Muscidae/*parasitology; Polymerase Chain Reaction; Polymorphism, Restriction Fragment Length; Spirurida Infections/parasitology/veterinary; Thelazioidea/chemistry/*genetics |
| Abstract |
Equine thelaziosis caused by the eyeworm Thelazia lacrymalis is a parasitic disease transmitted by muscid flies. Although equine thelaziosis is known to have worldwide distribution, information on the epidemiology and presence of the intermediate hosts of T. lacrymalis is lacking. In the present work, a PCR-RFLP based assay on the first and/or second internal transcribed spacer (ITS1 and ITS2) of ribosomal DNA was developed for the detection of T. lacrymalis DNA in its putative vector(s). The sensitivity of the technique was also assessed. The restriction patterns obtained readily differentiated T. lacrymalis from four species of Musca (Diptera, Muscidae) (i.e. Musca autumnalis, Musca domestica, Musca larvipara and Musca osiris), which are potential vectors of equine eyeworms. The molecular assay presented herein is a useful tool to identify the intermediate host(s) of T. lacrymalis in natural conditions and to study its/their ecology and epidemiology. |
| Address |
Department of Biomedical Comparative Sciences, Faculty of Veterinary Medicine, University of Teramo, Piazza Aldo Moro 45, 64100 Teramo, Italy. dtraversa@unite.it |
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English |
Summary Language |
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Series Issue |
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Edition |
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| ISSN |
0890-8508 |
ISBN |
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| Notes |
PMID:16038792 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
2626 |
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| Author |
Chiba, K.; Ikai, A.; Kawamura-Konishi, Y.; Kihara, H. |
| Title |
Kinetic study on myoglobin refolding monitored by five optical probe stopped-flow methods |
Type |
Journal Article |
| Year |
1994 |
Publication |
Proteins |
Abbreviated Journal |
Proteins |
| Volume |
19 |
Issue |
2 |
Pages |
110-119 |
| Keywords |
Animals; Chromatography, Gel; Circular Dichroism; Horses; Kinetics; Metmyoglobin/analogs & derivatives/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Urea |
| Abstract |
The refolding kinetics of horse cyanometmyoglobin induced by concentration jump of urea was investigated by five optical probe stopped-flow methods: absorption at 422 nm, tryptophyl fluorescence at around 340 nm, circular dichroism (CD) at 222 nm, CD at 260 nm, and CD at 422 nm. In the refolding process, we detected three phases with rate constants of > 1 x 10(2) s-1, (4.5-9.3) s-1, and (2-5) x 10(-3) s-1. In the fastest phase, a substantial amount of secondary structure (approximately 40%) is formed within the dead time of the CD stopped-flow apparatus (10.7 ms). The kinetic intermediate populated in the fastest phase is shown to capture a hemindicyanide, suggesting that a “heme pocket precursor” recognized by hemindicyanide must be constructed within the dead time. In the middle phase, most of secondary and tertiary structures, especially around the captured hemindicyanide, have been constructed. In the slowest phase, we detected a minor structural rearrangement accompanying the ligand-exchange reaction in the fifth coordination of ferric iron. We present a possible model for the refolding process of myoglobin in the presence of the heme group. |
| Address |
Laboratory of Biodynamics, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Kanagawa, Japan |
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English |
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Series Issue |
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Edition |
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| ISSN |
0887-3585 |
ISBN |
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| Notes |
PMID:8090705 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3799 |
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| Author |
Steinhoff, H.J. |
| Title |
A continuous wave laser T-jump apparatus and its application to chemical reactions in hemoglobin single crystals |
Type |
Journal Article |
| Year |
1988 |
Publication |
Journal of Biochemical and Biophysical Methods |
Abbreviated Journal |
J Biochem Biophys Methods |
| Volume |
15 |
Issue |
6 |
Pages |
319-330 |
| Keywords |
Animals; Chemistry; Crystallization; *Heat; *Hemoglobins; Horses/blood; *Lasers; Methemoglobin; Solutions; Thermodynamics; Thiocyanates |
| Abstract |
A laser temperature jump apparatus is constructed where the T-jump is achieved by means of the direct absorption of continuous laser radiation of low intensity by a solid sample. The final temperature in the irradiated volume element is reached when the absorbed radiation power equals the dissipation of heat by heat conduction. The time range from the beginning of irradiation to the stationary state depends on the geometry of the irradiated volume element and is less than 10 ms. The heating laser beam is simultaneously used to detect the relaxation to the new chemical equilibrium in the sample. Relaxation processes with relaxation rates between 10(2) s-1 and less than 10(-3) s-1 on samples with volumes less than 10(-3) mm3 may be investigated using this T-jump method. One application of this method is the determination of reaction rates of ligand reactions in hemoglobin single crystals. Rate constants obtained for the reaction of thiocyanate with crystallized horse methemoglobin are presented. |
| Address |
Institut fur Biophysik, Ruhr-Universitat Bochum, F.R.G |
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English |
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Series Issue |
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Edition |
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| ISSN |
0165-022X |
ISBN |
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Conference |
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| Notes |
PMID:3379245 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3804 |
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| Author |
Gilmanshin, R.; Callender, R.H.; Dyer, R.B. |
| Title |
The core of apomyoglobin E-form folds at the diffusion limit |
Type |
Journal Article |
| Year |
1998 |
Publication |
Nature Structural Biology |
Abbreviated Journal |
Nat Struct Biol |
| Volume |
5 |
Issue |
5 |
Pages |
363-365 |
| Keywords |
Animals; Apoproteins/*chemistry; Diffusion; Horses; Myoglobin/*chemistry; *Protein Folding; Spectroscopy, Fourier Transform Infrared; Temperature |
| Abstract |
The E-form of apomyoglobin has been characterized using infrared and fluorescence spectroscopies, revealing a compact core with native like contacts, most probably consisting of 15-20 residues of the A, G and H helices of apomyoglobin. Fast temperature-jump, time-resolved infrared measurements reveal that the core is formed within 96 micros at 46 degrees C, close to the diffusion limit for loop formation. Remarkably, the folding pathway of the E-form is such that the formation of a limited number of native-like contacts is not rate limiting, or that the contacts form on the same time scale expected for diffusion controlled loop formation. |
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English |
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Series Issue |
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Edition |
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| ISSN |
1072-8368 |
ISBN |
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| Notes |
PMID:9586997 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3795 |
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| Author |
Carroll, J.; Murphy, C.J.; Neitz, M.; Hoeve, J.N.; Neitz, J. |
| Title |
Photopigment basis for dichromatic color vision in the horse |
Type |
Journal Article |
| Year |
2001 |
Publication |
Journal of Vision |
Abbreviated Journal |
J Vis |
| Volume |
1 |
Issue |
2 |
Pages |
80-87 |
| Keywords |
Adaptation, Physiological; Animals; Color Perception/*physiology; Cones (Retina)/chemistry/*physiology; Electroretinography; Horses/*physiology; Photic Stimulation; Phototransduction/physiology; Retinal Pigments/analysis/*physiology; Visual Perception/physiology |
| Abstract |
Horses, like other ungulates, are active in the day, at dusk, dawn, and night; and, they have eyes designed to have both high sensitivity for vision in dim light and good visual acuity under higher light levels (Walls, 1942). Typically, daytime activity is associated with the presence of multiple cone classes and color-vision capacity (Jacobs, 1993). Previous studies in other ungulates, such as pigs, goats, cows, sheep and deer, have shown that they have two spectrally different cone types, and hence, at least the photopigment basis for dichromatic color vision (Neitz & Jacobs, 1989; Jacobs, Deegan II, Neitz, Murphy, Miller, & Marchinton, 1994; Jacobs, Deegan II, & Neitz, 1998). Here, electroretinogram flicker photometry was used to measure the spectral sensitivities of the cones in the domestic horse (Equus caballus). Two distinct spectral mechanisms were identified and are consistent with the presence of a short-wavelength-sensitive (S) and a middle-to-long-wavelength-sensitive (M/L) cone. The spectral sensitivity of the S cone was estimated to have a peak of 428 nm, while the M/L cone had a peak of 539 nm. These two cone types would provide the basis for dichromatic color vision consistent with recent results from behavioral testing of horses (Macuda & Timney, 1999; Macuda & Timney, 2000; Timney & Macuda, 2001). The spectral peak of the M/L cone photopigment measured here, in vivo, is similar to that obtained when the gene was sequenced, cloned, and expressed in vitro (Yokoyama & Radlwimmer, 1999). Of the ungulates that have been studied to date, all have the photopigment basis for dichromatic color vision; however, they differ considerably from one another in the spectral tuning of their cone pigments. These differences may represent adaptations to the different visual requirements of different species. |
| Address |
Department of Cell Biology, Neurobiology & Anatomy, Medical College of Wisconsin, Milwaukee, WI, USA |
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English |
Summary Language |
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Series Issue |
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Edition |
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| ISSN |
1534-7362 |
ISBN |
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| Notes |
PMID:12678603 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
4060 |
| Permanent link to this record |
