| Records |
| 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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0002-7863 |
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| Notes |
PMID:11439052 |
Approved |
no |
Call Number  |
Equine Behaviour @ team @ |
Serial |
3788 |
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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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0021-9258 |
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| Notes |
PMID:6277891 |
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no |
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Equine Behaviour @ team @ |
Serial |
3807 |
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| 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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English |
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0014-2956 |
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| Notes |
PMID:7011796 |
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no |
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Equine Behaviour @ team @ |
Serial |
3810 |
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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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0021-9940 |
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no |
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Equine Behaviour @ team @ |
Serial |
5133 |
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| Author |
Massen, J.; Sterck, E.; de Vos, H. |
| Title |
Close social associations in animals and humans: functions and mechanisms of friendship |
Type |
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| Year |
2010 |
Publication |
Behaviour |
Abbreviated Journal |
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| Volume |
147 |
Issue |
11 |
Pages |
1379 |
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Both humans and group-living animals associate and behave affiliatively more with some individuals than others. Human friendship has long been acknowledged, and recently scientists studying animal behaviour have started using the term friendship for close social associates in animals. Yet, while biologists describe friends as social tools to enhance fitness, social scientists describe human friendship as unconditional. We investigate whether these different descriptions reflect true differences in human friendship and animal close social associations or are a by-product of different research approaches: namely social scientists focussing on proximate and biologists on ultimate explanations. We first stress the importance of similar measures to determine close social associations, thereafter examine their ultimate benefits and proximate motivations, and discuss the latest findings on the central-neural regulation of social bonds. We conclude that both human friendship and animal close social associations are ultimately beneficial. On the proximate level, motivations for friendship in humans and for close social associations in animals are not necessarily based on benefits and are often unconditional. Moreover, humans share with many animals a similar physiological basis of sociality. Therefore, biologists and social scientist describe the same phenomenon, and the use of the term friendship for animals seems justified. |
| Abstract |
Both humans and group-living animals associate and behave affiliatively more with some individuals than others. Human friendship has long been acknowledged, and recently scientists studying animal behaviour have started using the term friendship for close social associates in animals. Yet, while biologists describe friends as social tools to enhance fitness, social scientists describe human friendship as unconditional. We investigate whether these different descriptions reflect true differences in human friendship and animal close social associations or are a by-product of different research approaches: namely social scientists focussing on proximate and biologists on ultimate explanations. We first stress the importance of similar measures to determine close social associations, thereafter examine their ultimate benefits and proximate motivations, and discuss the latest findings on the central-neural regulation of social bonds. We conclude that both human friendship and animal close social associations are ultimately beneficial. On the proximate level, motivations for friendship in humans and for close social associations in animals are not necessarily based on benefits and are often unconditional. Moreover, humans share with many animals a similar physiological basis of sociality. Therefore, biologists and social scientist describe the same phenomenon, and the use of the term friendship for animals seems justified. |
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Equine Behaviour @ team @ |
Serial |
5813 |
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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 |
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Equine Behaviour @ team @ |
Serial |
5964 |
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| Author |
Reyna-Garfias, H.; Miliar, A.; Jarillo-Luna, A.; Rivera-Aguilar, V.; Pacheco-Yepez, J.; Baeza, I.; Campos-Rodríguez, R. |
| Title |
Repeated restraint stress increases IgA concentration in rat small intestine |
Type |
Journal Article |
| Year |
2010 |
Publication |
Brain, Behavior, and Immunity |
Abbreviated Journal |
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| Volume |
24 |
Issue |
1 |
Pages |
110-118 |
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Restraint-stress; IgA; Small intestine; Polymeric Ig receptor; Catecholamines; Glucocorticoids |
| Abstract |
The most abundant intestinal immunoglobulin and first line of specific immunological defense against environmental antigens is secretory immunoglobulin A. To better understand the effect of repeated stress on the secretion of intestinal IgA, the effects of restraint stress on IgA concentration and mRNA expression of the gene for the alpha-chain of IgA was assessed in both the duodenum and ileum of the rats. Restraint stress induced an increase in intestinal IgA, which was blocked by an adrenalectomy, suggesting a role of catecholamines and glucocorticoids. Whereas the blocking of glucocorticoid receptors by RU-486 did not affect the increased IgA concentration, it did reduce IgA alpha-chain mRNA expression in both segments, indicating a possible mediation on the part of glucocorticoids in IgA secretion by individual cells. Treatment with corticosterone significantly increased both the IgA concentration and IgA alpha-chain mRNA expression in ileum but not in duodenum, suggesting that glucocorticoids may act directly on IgA-antibody forming cells to increase IgA secretion in the former segment. A probable role by catecholamines was evidenced by the reduction in IgA concentration and IgA alpha-chain mRNA expression in both segments after a chemical sympathectomy with 6-hydroxydopamine (6-OHDA). Additionally, norepinephrine significantly reduced IgA alpha-chain mRNA levels but increased pIgR mRNA expression and IgA concentration in both intestinal segments. We propose that the increased intestinal IgA levels caused by repeated restraint stress is likely due to the effects of catecholamines on the transport of plgA across the epithelium. |
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0889-1591 |
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no |
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Equine Behaviour @ team @ |
Serial |
6002 |
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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 |
ISBN |
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Equine Behaviour @ team @ |
Serial |
5996 |
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Weber-Mzell, D.; Kotanko, P.; Hauer, A.C.; Goriup, U.; Haas, J.; Lanner, N.; Erwa, W.; Ahmaida, I.A.; Haitchi-Petnehazy, S.; Stenzel, M.; Lanzer, G.; Deutsch, J. |
| Title |
Gender, age and seasonal effects on IgA deficiency: a study of 7293 Caucasians |
Type |
Journal Article |
| Year |
2004 |
Publication |
European Journal of Clinical Investigation |
Abbreviated Journal |
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| Volume |
34 |
Issue |
3 |
Pages |
224-228 |
| Keywords |
Age- and gender-related variability; immunoglobulin A; seasonal variability; serum IgA deficiency |
| Abstract |
Background The frequency of serum IgA deficiency (SIgAD) differs between populations. We examined the prevalence of SIgAD in healthy Caucasians. Materials and methods Serum immunoglobulin A (SIgA) was measured in 7293 volunteers (2264 women, 5029 men) aged 30 ± 14·2 years (mean ± SD; range: 12–66). Serum immunoglobulin A and subnormal SIgA levels were defined by a SIgA level < 0·07 g L-1, and between 0·07 and 0·7 g L-1, respectively. Means were compared by analysis of variance (anova) and analysis of covariance (ancova); frequencies by the χ2 test. Results Fifteen subjects (0·21%; one woman, 14 men) had SIgAD. Subnormal SIgA levels were found in 155 persons (2·13%): 21 females (0·93% of the females) and 134 males (2·66% of the males; difference: 1·74%; 95% CI: 1·12–2·33%; P < 0·001). Males were more likely to have subnormal SIgA levels or SIgAD (odds ratio 3·09, 95% CI: 1·97–4·85). The prevalence of SIgAD and subnormal SIgA was lowest in winter (χ2 = 14·8; P = 0·002; 3 d.f.; and χ2 = 43·2; P < 0·001; 3 d.f., respectively). Serum immunoglobulin A concentrations were significantly higher during winter. Serum immunoglobulin A levels increased with age on average by 0·2 ± 0·06 g L-1 per decade of life (P < 0·001). Taking into account the influence of age, SIgA concentration was lower in females as compared with males. Conclusion The prevalence of SIgAD and subnormal SIgA levels is increased in males. There exists a significant influence of gender, age and seasons on SIgA levels. |
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Blackwell Science Ltd |
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Edition |
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1365-2362 |
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no |
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Equine Behaviour @ team @ |
Serial |
6127 |
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| Author |
Palm, A.-K.E.; Wattle, O.; Lundström, T.; Wattrang, E. |
| Title |
Secretory immunoglobulin A and immunoglobulin G in horse saliva |
Type |
Journal Article |
| Year |
2016 |
Publication |
Veterinary Immunology and Immunopathology |
Abbreviated Journal |
Vet. Immunol. Immunolpathol. |
| Volume |
180 |
Issue |
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Pages |
59-65 |
| Keywords |
Equine; Secretory IgA; IgG; Saliva; Mucosal immunity |
| Abstract |
This study aimed to increase the knowledge on salivary antibodies in the horse since these constitute an important part of the immune defence of the oral cavity. For that purpose assays to detect horse immunoglobulin A (IgA) including secretory IgA (SIgA) were set up and the molecular weights of different components of the horse IgA system were estimated. Moreover, samples from 51 clinically healthy horses were tested for total SIgA and IgG amounts in saliva and relative IgG3/5 (IgG(T)) and IgG4/7 (IgGb) content were tested in serum and saliva. Results showed a mean concentration of 74μg SIgA/ml horse saliva and that there was a large inter-individual variation in salivary SIgA concentration. For total IgG the mean concentration was approx. 5 times lower than that of SIgA, i.e. 20μg IgG/ml saliva and the inter-individual variation was lower than that observed for SIgA. The saliva-serum ratio for IgG isotypes IgG3/5 and IgG4/7 was also assessed in the sampled horses and this analysis showed that the saliva-serum ratio of IgG4/7 was in general approximately 4 times higher than that of IgG3/5. The large inter-individual variation in salivary SIgA levels observed for the normal healthy horses in the present study emphasises the need for a large number of observations when studying this parameter especially in a clinical setting. Moreover, our results also indicated that some of the salivary IgG does not originate from serum but may be produced locally. Thus, these results provide novel insight, and a base for further research, into salivary antibody responses of horses. |
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0165-2427 |
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Equine Behaviour @ team @ |
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6514 |
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