Records |
Author |
Andersson, P.; Kvassman, J.; Lindstrom, A.; Olden, B.; Pettersson, G. |
Title |
Effect of NADH on the pKa of zinc-bound water in liver alcohol dehydrogenase |
Type |
Journal Article |
Year |
1981 |
Publication |
European Journal of Biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
Volume |
113 |
Issue |
3 |
Pages |
425-433 |
Keywords |
Alcohol Oxidoreductases/*metabolism; Aldehydes/metabolism; Animals; Binding Sites; Cinnamates/metabolism; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Liver/*metabolism; NAD/*metabolism; Water/metabolism; Zinc/metabolism |
Abstract |
Equilibrium constants for coenzyme binding to liver alcohol dehydrogenase have been determined over the pH range 10--12 by pH-jump stop-flow techniques. The binding of NADH or NAD+ requires the protonated form of an ionizing group (distinct from zinc-bound water) with a pKa of 10.4. Complex formation with NADH exhibits an additional dependence on the protonation state of an ionizing group with a pKa of 11.2. The binding of trans-N,N-dimethylaminocinnamaldehyde to the enzyme . NADH complex is prevented by ionization of the latter group. It is concluded from these results that the pKa-11.2-dependence of NADH binding most likely derives from ionization of the water molecule bound at the catalytic zinc ion of the enzyme subunit. The pKa value of 11.2 thus assigned to zinc-bound water in the enzyme . NADH complex appears to be typical for an aquo ligand in the inner-sphere ligand field provided by the zinc-binding amino acid residues in liver alcohol dehydrogenase. This means that the pKa of metal-bound water in zinc-containing enzymes can be assumed to correlate primarily with the number of negatively charged protein ligands coordinated by the active-site zinc ion. |
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0014-2956 |
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PMID:7011796 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
3810 |
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Author |
Dyson, H.J.; Beattie, J.K. |
Title |
Spin state and unfolding equilibria of ferricytochrome c in acidic solutions |
Type |
Journal Article |
Year |
1982 |
Publication |
The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
Volume |
257 |
Issue |
5 |
Pages |
2267-2273 |
Keywords |
Animals; *Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium; Protein Binding; Protein Conformation; Spectrophotometry; Temperature |
Abstract |
Equilibrium, stopped flow, and temperature-jump spectrophotometry have been used to identify processes in the unfolding of ferricytochrome c in acidic aqueous solutions. A relaxation occurring in approximately 100 microseconds involves perturbation of a spin-equilibrium between two folded conformers of the protein with methionine-80 coordinated or dissociated from the heme iron. The protein unfolds more slowly, in milliseconds, with dissociation and protonation of histidine-18. These two transitions appear cooperative in equilibrium measurements at low (0.01 M) ionic strength, but are separated at higher (0.10 M) ionic strength. They are resolved under both conditions in the dynamic measurements. The spin-equilibrium description permits a unified explanation of a number of properties of ferricytochrome c in acidic aqueous solutions. |
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ISSN |
0021-9258 |
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Notes |
PMID:6277891 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
3807 |
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Author |
Thor, D.H.; Holloway, W.R. |
Title |
Social memory of the male laboratory rat |
Type |
Journal Article |
Year |
1982 |
Publication |
Journal of Comparative and Physiological Psychology |
Abbreviated Journal |
J. Comp. Physiol. Psychol. |
Volume |
96 |
Issue |
6 |
Pages |
1000-1006 |
Keywords |
duration of social-investigatory behavior, measure of conspecific recognition &; social memory, male rats |
Abstract |
Used duration of social-investigatory behavior by 36 mature male Long-Evans rats as a measure of individual recognition in 5 experiments to assess social memory. In Exp I, the duration of social investigation during a 2nd exposure to the same juvenile (n[en space]=[en space]12) was directly related to the length of the interexposure interval. In Exp II, Ss were exposed to the same or different juvenile 10 min after an initial 5-min exposure to a novel juvenile; reexposure to the same juvenile elicited significantly less social investigation than an exposure to a different juvenile. Exps III and IV demonstrated that following a 5-min introductory exposure, social memory of the juvenile was relatively brief in comparison with that of mature Ss. Exp V revealed a retroactive interference effect on recently acquired memory for an individual: 12 mature Ss exposed to interpolated social experience engaged in significantly longer investigation of a juvenile than those with no interpolated social experience. The combined results suggest that (1) the rat normally engages in spontaneous learning of individual identity and (2) social memory may be a significant aspect of complex social interactions. (16 ref) (PsycINFO Database Record (c) 2006 APA, all rights reserved) |
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ISSN |
0021-9940 |
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Equine Behaviour @ team @ |
Serial |
5133 |
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Author |
Hertsch, B.; Becker, C. |
Title |
[Occurrence of aseptic necrosis of the palmar and plantar ligament in the horse--a contribution to the differentiation of sesamoid bone diseases] |
Type |
Journal Article |
Year |
1986 |
Publication |
DTW. Deutsche tierarztliche Wochenschrift |
Abbreviated Journal |
Dtsch Tierarztl Wochenschr |
Volume |
93 |
Issue |
6 |
Pages |
263-266 |
Keywords |
Animals; Diagnosis, Differential; Horse Diseases/*pathology; Horses; Ligaments, Articular/*pathology; Osteonecrosis/*pathology; Sesamoid Bones/*pathology |
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Language |
German |
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Original Title |
Zum Vorkommen der aseptischen Nekrose im Ligamentum palmare bzw. plantare beim Pferd--ein Beitrag zur Differenzierung der Gleichbeinerkrankungen |
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ISSN |
0341-6593 |
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Notes |
PMID:3527654 |
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no |
Call Number |
refbase @ user @ |
Serial |
150 |
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Author |
Skandakumar, S.; Stodulski, G.; Hau, J. |
Title |
Salivary IgA: a Possible Stress Marker In Dogs |
Type |
Abstract |
Year |
1995 |
Publication |
Animal Welfare |
Abbreviated Journal |
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Volume |
4 |
Issue |
4 |
Pages |
339-350 |
Keywords |
Animal Welfare; Behaviour; Cortisol; Dog; Salivary Iga (S-Iga); Stress; Well-Being |
Abstract |
Stress in humans has been reported to be associated with a decrease in the salivary immunoglobulin A (s-IgA) levels enabling the possible use of s-IgA to assess stress. Prolonged stress, if reliably assessed in a non-invasive manner, may be used to assess animal welfare. This study analysed groups of dogs undergoing physical and temperamental training and s-IgA levels were measured by rocket immunoelectrophoresis in prospective samples. Behavioural assessment was carried out and cortisol levels in saliva were measured by ELISA. A significant negative correlation (P < 0.007) between the logarithmic cortisol concentrations and s-IgA levels in saliva was recorded. The behavioural assessment of the dogs agreed well with the biochemical markers. It is concluded that IgA levels in saliva may be a useful marker of dog well-being and that stress results in decreased s-IgA levels. |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
5964 |
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Author |
Vetvik, H.; Grewal, H.M.S.; Haugen, I.L.; Åhrén, C.; Haneberg, B. |
Title |
Mucosal antibodies can be measured in air-dried samples of saliva and feces |
Type |
Journal Article |
Year |
1998 |
Publication |
Journal of Immunological Methods |
Abbreviated Journal |
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Volume |
215 |
Issue |
1–2 |
Pages |
163-172 |
Keywords |
Saliva; Feces; IgA; IgG; Air-drying |
Abstract |
IgA antibodies reflecting airways or intestinal mucosal immune responses can be found in saliva and feces, respectively, and IgG antibodies reflecting serum antibodies can be found in saliva. In this study, antibodies were detected in samples of saliva and feces which had been air-dried at room temperature (+20°C) or +37°C, and stored at these temperatures for up to 6 months. In saliva the antibody levels increased, while the antibodies in feces decreased upon storage. The individual IgA antibody concentrations which were adjusted by using the ratios of specific IgA/total IgA were relatively stable in both saliva and feces, and correlated with corresponding antibody levels in samples which had been stored at -20°C. The results indicate that air-dried saliva and feces can be used for semiquantitative measurements of mucosal antibodies, even after prolonged storage at high temperatures and lack of refrigeration. |
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0022-1759 |
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no |
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Equine Behaviour @ team @ |
Serial |
5996 |
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Author |
Meershoek, L.S.; Schamhardt, H.C.; Roepstorff, L.; Johnston, C. |
Title |
Forelimb tendon loading during jump landings and the influence of fence height |
Type |
Journal Article |
Year |
2001 |
Publication |
Equine Veterinary Journal. Supplement |
Abbreviated Journal |
Equine Vet J Suppl |
Volume |
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Issue |
33 |
Pages |
6-10 |
Keywords |
Animals; Biomechanics; Forelimb/injuries/physiology; Horses/injuries/*physiology; Lameness, Animal/etiology; Ligaments, Articular/*physiology; Locomotion/*physiology; Physical Conditioning, Animal; Tendon Injuries/complications/physiopathology/veterinary; Tendons/*physiology; Weight-Bearing/physiology |
Abstract |
Lameness in athletic horses is often caused by forelimb tendon injuries, especially in the interosseus tendon (TI) and superficial digital flexor tendon (SDF), but also in the accessory ligament (AL) of the deep digital flexor tendon (DDF). In an attempt to explain the aetiology of these injuries, the present study investigated the loading of the tendons during landing after a jump. In jumping horses, the highest forces can be expected in the trailing limb during landing. Therefore, landing kinematics and ground reaction forces of the trailing forelimb were measured from 6 horses jumping single fences with low to medium heights of 0.80, 1.00 and 1.20 m. The tendon forces were calculated using inverse dynamics and an in vitro model of the lower forelimb. Calculated peak forces in the TI, SDF and DDF + AL during landing were 15.8, 13.9 and 11.7 kN respectively. The relative loading of the tendons (landing forces compared with failure forces determined in a separate study) increased from DDF to TI to SDF and was very high in SDF. This explains the low injury incidence of the DDF and the high injury incidence of the SDF. Fence height substantially influenced SDF forces, whereas it hardly influenced TI forces and did not influence AL strain. Reduction of fence height might therefore limit the risks for SDF injuries, but not for TI and AL injuries. |
Address |
Department of Veterinary Anatomy and Physiology, Institute for Fundamental and Clinical Human Movement Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands |
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PMID:11721571 |
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no |
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Equine Behaviour @ team @ |
Serial |
3786 |
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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 |
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English |
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ISSN |
0002-7863 |
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PMID:11439052 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
3788 |
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Author |
Rollot, Y.; Lecuyer, E.; Chateau, H.; Crevier-Denoix, N. |
Title |
Development of a 3D model of the equine distal forelimb and of a GRF shoe for noninvasive determination of in vivo tendon and ligament loads and strains |
Type |
Journal Article |
Year |
2004 |
Publication |
Equine Veterinary Journal |
Abbreviated Journal |
Equine Vet J |
Volume |
36 |
Issue |
8 |
Pages |
677-682 |
Keywords |
Animals; Biomechanics; Floors and Floorcoverings; Forelimb/*physiology/ultrasonography; Gait/physiology; Horses/*physiology; Image Processing, Computer-Assisted; Imaging, Three-Dimensional/methods/*veterinary; Ligaments, Articular/*physiology; Locomotion/*physiology; Models, Biological; Shoes; Tendons/*physiology; Toe Joint/physiology/ultrasonography |
Abstract |
REASONS FOR PERFORMING STUDY: As critical locomotion events (e.g. high-speed and impacts during racing, jump landing) may contribute to tendinopathies, in vivo recording of gaits kinematic and dynamic parameters is essential for 3D reconstruction and analysis. OBJECTIVE: To propose a 3D model of the forelimb and a ground reaction force recording shoe (GRF-S) for noninvasively quantifying tendon and ligament loads and strains. METHODS: Bony segments trajectories of forelimbs placed under a power press were recorded using triads of ultrasonic kinematic markers linked to the bones. Compression cycles (from 500-6000 N) were applied for different hoof orientations. Locations of tendon and ligament insertions were recorded with regard to the triads. The GRF-S recorded GRF over the hoof wall and used four 3-axis force sensors sandwiched between a support shoe and the shoe to be tested. RESULTS: Validation of the model by comparing calculated and measured superficial digital flexor tendon strains, and evaluation of the role of proximal interphalangeal joint in straight sesamoidean ligament and oblique sesamoidean ligament strains, were successfully achieved. Objective comparisons of the 3 components of GRF over the hoof for soft and hard grounds could be recorded, where the s.d. of GRF norm was more important on hard ground at walk and trot. CONCLUSIONS: Soft grounds (sand and rubber) dissipate energy by lowering GRF amplitude and diminish bounces and vibrations at impact. At comparable speed, stance phase was longer on soft sand ground. POTENTIAL RELEVANCE: The conjugate use of the GRF-S and the numerical model would help to quantify and analyse ground/shoe combination on comfort, propulsion efficiency or lameness recovery. |
Address |
UMR INRA-ENVA de Biomecanique et Pathologie Locomotrice du Cheval, Ecole Nationale Veterinaire d'Alfort, 7, Avenue du General de Gaulle, 94704 Maisons-Alfort, France |
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0425-1644 |
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PMID:15656495 |
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no |
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Equine Behaviour @ team @ |
Serial |
3769 |
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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 |
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Edition |
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ISSN |
1572-3887 |
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PMID:15648974 |
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no |
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Equine Behaviour @ team @ |
Serial |
3770 |
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