| Records |
| Author |
Anderson, W.D.; Summers, C.H. |
| Title |
Neuroendocrine Mechanisms, Stress Coping Strategies, and Social Dominance: Comparative Lessons about Leadership Potential |
Type |
Journal Article |
| Year |
2007 |
Publication |
The ANNALS of the American Academy of Political and Social Science |
Abbreviated Journal |
Ann Am Acad Polit Soc Sci |
| Volume |
614 |
Issue |
1 |
Pages |
102-130 |
Keywords  |
social dominance – authoritarian – Five Factor Model – neurochemistry – neurotransmitters – leadership |
| Abstract |
The authors examine dominance and subordination in the social psychology, political science, and biology literatures. Using Summers and Winberg (2006) as a guide, the authors suggest that extreme dominance or subordination phenotypes--including social dominance orientation and right-wing authoritarianism--are determined by an organism's genetic predispositions, motivations, stress responses, and long-term hormone release and uptake states. The authors offer hypotheses about the likely neurochemical profiles for each of these extreme dominance and subordination phenotypes and suggest two designs that begin to test these hypotheses. |
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no |
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Equine Behaviour @ team @ |
Serial |
4699 |
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| Author |
Reynhout, I.C.; Cornelissen, J.J.L.M.; Nolte, R.J.M. |
| Title |
Self-assembled architectures from biohybrid triblock copolymers |
Type |
Journal Article |
| Year |
2007 |
Publication |
Journal of the American Chemical Society |
Abbreviated Journal |
J Am Chem Soc |
| Volume |
129 |
Issue |
8 |
Pages |
2327-2332 |
| Keywords |
Horseradish Peroxidase/*chemistry; Micelles; Molecular Structure; Myoglobin/*chemistry; Particle Size; Polyethylene Glycols/*chemistry; Polymers/*chemical synthesis/chemistry; Polystyrenes/*chemistry; Surface-Active Agents/chemical synthesis/chemistry |
| Abstract |
The synthesis and self-assembly behavior of biohybrid ABC triblock copolymers consisting of a synthetic diblock, polystyrene-b-polyethylene glycol (PSm-b-PEG113), where m is varied, and a hemeprotein, myoglobin (Mb) or horse radish peroxidase (HRP), is described. The synthetic diblock copolymer is first functionalized with the heme cofactor and subsequently reconstituted with the apoprotein or the apoenzyme to yield the protein-containing ABC triblock copolymer. The obtained amphiphilic block copolymers self-assemble in aqueous solution into a large variety of aggregate structures. Depending on the protein and the polystyrene block length, micellar rods, vesicles, toroids, figure eight structures, octopus structures, and spheres with a lamellar surface are formed. |
| Address |
Institute for Molecules and Materials, Radboud University Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands |
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English |
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Series Issue |
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Edition |
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| ISSN |
0002-7863 |
ISBN |
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| Notes |
PMID:17274615 |
Approved |
no |
| Call Number |
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Serial |
1832 |
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| 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 |
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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 |
Aviad, A.D.; Houpt, J.B. |
| Title |
The molecular weight of therapeutic hyaluronan (sodium hyaluronate): how significant is it? |
Type |
Journal Article |
| Year |
1994 |
Publication |
The Journal of rheumatology |
Abbreviated Journal |
J Rheumatol |
| Volume |
21 |
Issue |
2 |
Pages |
297-301 |
| Keywords |
Animals; Horse Diseases/drug therapy; Horses; Humans; Hyaluronic Acid/*chemistry/*therapeutic use; Joint Diseases/*drug therapy/veterinary; Molecular Weight; Osteoarthritis/drug therapy/veterinary; Synovial Fluid/drug effects/physiology; Viscosity |
| Abstract |
Various molecular weight hyaluronic acid (HA) preparations have been injected into joints for the treatment of human and equine osteoarthritis. A therapeutic advantage has been claimed for commercial products with a molecular weight in the range found in normal synovial fluid (SF), compared to lower molecular weight products. But a correlation between molecular weight and efficacy is not borne out by an analysis of the available literature on clinical results. SF viscosity, HA concentration, HA molecular weight and rate of synthesis in joint disease. It is proposed that the beneficial effect of injected HA in joint disease may be due to pharmacological rather than to physical properties. |
| Address |
Rheumatic Disease Unit, Mount Sinai Hospital, University of Toronto, ON, Canada |
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English |
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0315-162X |
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| Notes |
PMID:8182640 |
Approved |
no |
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refbase @ user @ |
Serial |
35 |
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| Author |
Palme, R. |
| Title |
Measuring fecal steroids: guidelines for practical application |
Type |
Journal Article |
| Year |
2005 |
Publication |
Annals of the New York Academy of Sciences |
Abbreviated Journal |
Ann N Y Acad Sci |
| Volume |
1046 |
Issue |
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Pages |
75-80 |
| Keywords |
Animals; Feces/*chemistry; Immunoassay/methods; Reproducibility of Results; Specimen Handling/methods; Steroids/*analysis |
| Abstract |
During the past 20 years, measuring steroid hormone metabolites in fecal samples has become a widely appreciated technique, because it has proved to be a powerful, noninvasive tool that provides important information about an animal's endocrine status (adrenocortical activity and reproductive status). However, although sampling is relatively easy to perform and free of feedback, a careful consideration of various factors is necessary to achieve proper results that lead to sound conclusions. This article aims to provide guidelines for an adequate application of these techniques. It is meant as a checklist that addresses the main topics of concern, such as sample collection and storage, time delay extraction procedures, assay selection and validation, biological relevance, and some confounding factors. These issues are discussed briefly here and in more detail in other recent articles. |
| Address |
Institute of Biochemistry, Department of Natural Sciences, University of Veterinary Medicine, Veterinaerplatz 1, A-1210 Vienna, Austria. Rupert.Palme@vu-wien.ac.at |
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English |
Summary Language |
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Series Issue |
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Edition |
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| ISSN |
0077-8923 |
ISBN |
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| Notes |
PMID:16055844 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
4081 |
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| Author |
Schwarzenberger, F.; Mostl, E.; Bamberg, E.; Pammer, J.; Schmehlik, O. |
| Title |
Concentrations of progestagens and oestrogens in the faeces of pregnant Lipizzan, trotter and thoroughbred mares |
Type |
Journal Article |
| Year |
1991 |
Publication |
Journal of reproduction and fertility. Supplement |
Abbreviated Journal |
J Reprod Fertil Suppl |
| Volume |
44 |
Issue |
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Pages |
489-499 |
| Keywords |
Animals; Estrogens/*analysis; Feces/*chemistry; Female; Gestational Age; Horses/*metabolism; Immunoenzyme Techniques; Labor, Obstetric; Pregnancy; Pregnancy, Animal/*metabolism; Pregnenes/analysis; Progestins/*analysis |
| Abstract |
Faecal samples were collected at weekly intervals from pregnant Lipizzan mares during Weeks 7-16 following mating and from Lipizzan, Trotter and Thoroughbred mares during the last 3 months of gestation. After parturition, samples were taken daily from the Thoroughbred mares for another 6 days. Non-pregnant mares served as controls. The concentrations of unconjugated oestrogens (Eg), 20 alpha-OH-progestagens (20 alpha-G) and 20 beta-OH-progestagens (20 beta-G) were measured by enzyme immunoassay. In the faeces of Lipizzan mares, immunoreactive progestagens were significantly (P less than 0.01) elevated above the levels in non-pregnant mares by Week 11, and Eg by Week 13 of pregnancy onwards. During the last 3 months of gestation, concentrations of Eg were significantly higher in Trotter mares than in Lipizzan and Thoroughbred mares. Concentrations of 20 alpha-G and 20 beta-G increased to maximal values in the last month of gestation. There was no significant difference among the 3 breeds with respect to 20 alpha-G but, during the 10 weeks before parturition, concentrations of 20 beta-G in the Lipizzan mares were significantly lower (P less than 0.05) than those in the Thoroughbred mares. They were also significantly lower than those of the Trotter mares during the last 4 weeks of gestation. After parturition, the concentrations of Eg and progestagens had declined to baseline values by Days 3 and 4 respectively. From these results we conclude that high concentrations of progestagens with 20 alpha- and 20 beta-hydroxyl groups are present in the faeces of pregnant mares, especially during the last month of gestation. |
| Address |
Institut fur Biochemie, Veterinary Medical University, Vienna, Austria |
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Place of Publication |
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English |
Summary Language |
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Original Title |
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Abbreviated Series Title |
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Edition |
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| ISSN |
0449-3087 |
ISBN |
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| Notes |
PMID:1795293 |
Approved |
no |
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refbase @ user @ |
Serial |
322 |
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| Author |
Traversa, D.; Giangaspero, A.; Iorio, R.; Otranto, D.; Paoletti, B.; Gasser, R.B. |
| Title |
Semi-nested PCR for the specific detection of Habronema microstoma or Habronema muscae DNA in horse faeces |
Type |
Journal Article |
| Year |
2004 |
Publication |
Parasitology |
Abbreviated Journal |
Parasitology |
| Volume |
129 |
Issue |
Pt 6 |
Pages |
733-739 |
| Keywords |
Animals; DNA, Helminth/*analysis; DNA, Ribosomal Spacer/*chemistry; Feces/*chemistry; Female; Horse Diseases/*diagnosis/parasitology; Horses; Male; Polymerase Chain Reaction/*methods; Species Specificity; Spirurida Infections/diagnosis/*veterinary; Spiruroidea/*genetics |
| Abstract |
Habronema microstoma and Habronema muscae (Spirurida: Habronematidae) are parasitic nematodes which infect the stomach and/or skin of equids. The accurate diagnosis of gastric habronemosis is central to studying its epidemiology, but data on its distribution and prevalence are lacking, mainly due to the limitations of clinical and coprological diagnosis in live horses. To overcome this constraint, a two-step, semi-nested PCR-based assay was validated (utilizing genetic markers in the nuclear ribosomal DNA) for the specific amplification of H. microstoma or H. muscae DNA from the faeces from horses (n = 46) whose gastrointestinal parasite status had been determined at autopsy and whose faeces were examined previously using a conventional parasitological approach. Of these horses examined at autopsy, some harboured adults of either H. microstoma (n= 19) or H. muscae (n =4), and others (n = 7) harboured both species. Most of them were also infected with other parasites, including strongylid nematodes (subfamilies Cyathostominae and Strongylinae), bots and/or cestodes; there was no evidence of metazoan parasites in 2 horses. Larvated spirurid eggs were detected in the faeces of 1 of the 30 horses (3.3 %) shown to be infected with Habronema at autopsy. For this set of 46 samples, the PCR assay achieved a diagnostic specificity of 100 % and a sensitivity of approximately 97 % (being able to specifically detect as little as approximately 0.02 fg of Habronema DNA). The specificity of the assay was also tested using a panel of control DNA samples representing horse, the gastric spirurid Draschia megastoma and 26 other species of parasites from the alimentary tract of the horse. H. microstoma, H. muscae and D. megastoma could be readily differentiated from one another based on the sizes of their specific amplicons in the PCR. The results of this study showed that the performance of the PCR for the diagnosis of gastric habronemosis was similar to that of autopsy but substantially better than the traditional coprological examination procedure used. The ability to specifically diagnose gastric habronemosis in equids should have important implications for investigating the epidemiology and ecology of H. microstoma and H. muscae. |
| Address |
Department of Biomedical Comparative Sciences, Faculty of Veterinary Medicine, University of Teramo, Teramo, Italy. traversa@unite.it |
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English |
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0031-1820 |
ISBN |
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| Notes |
PMID:15648696 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
2631 |
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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 |
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English |
Summary Language |
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Edition |
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1572-3887 |
ISBN |
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| Notes |
PMID:15648974 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3770 |
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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 |
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English |
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Series Issue |
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Edition |
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0022-2836 |
ISBN |
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| Notes |
PMID:12875834 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3781 |
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| Author |
Steinhoff, H.J.; Schrader, J.; Schlitter, J. |
| Title |
Temperature-jump studies and polarized absorption spectroscopy of methemoglobin-thiocyanate single crystals |
Type |
Journal Article |
| Year |
1992 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
| Volume |
1121 |
Issue |
3 |
Pages |
269-278 |
| Keywords |
Animals; Crystallization; Horses; Kinetics; Methemoglobin/*chemistry; Solutions; Spectrum Analysis; Temperature; Thiocyanates/*chemistry |
| Abstract |
Association equilibria and association kinetics of the thiocyanate binding reaction to methemoglobin in single crystals and solution are studied using temperature-jump technique and polarized absorption spectroscopy. Different kinetic constants are found for the reaction in solution and crystal phase for the alpha- and beta-subunits of the methemoglobin tetramer. The reduction of the reactivity of the alpha- and beta-subunits in crystalline phase is 6-fold and 2.4-fold, respectively, compared to the values found in solution. The intramolecular binding reaction of the N epsilon of the distal histidine E7 which is observed in methemoglobin in solution cannot be detected in single crystals. Our results suggest that crystallization of hemoglobin has little influence on small-scale structural fluctuations which are necessary for ligands to get to the binding sites and large-scale structural motions are suppressed. |
| Address |
Institut fur Biophysik, Ruhr-Universitat Bochum, Germany |
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Place of Publication |
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Editor |
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English |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0006-3002 |
ISBN |
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Medium |
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Expedition |
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Conference |
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| Notes |
PMID:1627604 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3800 |
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