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Golynski, M., Szczepanik, M. P., Wilkolek, P. M., Adamek, L. R., Sitkowski, W., & Taszkun, I. (2018). Influence of hair clipping on transepidermal water loss values in horses: a pilot study. Polish Journal of Veterinary Sciences, vol. 21(No 1).
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Maury, M., Murphy, K., Kumar, S., Mauerer, A., & Lee, G. (2005). Spray-drying of proteins: effects of sorbitol and trehalose on aggregation and FT-IR amide I spectrum of an immunoglobulin G. Eur. J. Pharm. Biopharm., 59(2), 251–261.
Abstract: An immunoglobulin G (IgG) was spray-dried on a Büchi 190 laboratory spray-dryer at inlet and outlet air temperatures of 130 and 190°C, respectively. The IgG solution contains initially 115mg/ml IgG plus 50mg/ml sorbitol. After dialysis, at least 80% of low molecular weight component was removed. After spray-drying the dialyzed IgG and immediate redissolution of the powder, an increase in aggregates from 1 to 17% occurred. A major shift towards increase β-sheet structure was detected in the spray-dried solid, which, however, reverted to native structure on redissolution of the powder. A correlation between aggregation determined by size exclusion chromatography and alterations in secondary structure determined by Fourier transformation infra-red spectroscopy could not therefore be established. On spray-drying a non-dialyzed, sorbitol-containing IgG only some 0.7% aggregates were formed. The sorbitol is therefore evidently able to stabilize partially the IgG during the process of spray-drying. Addition of trehalose to the liquid feed produced quantitatively the same stabilizing action on the IgG during spray-drying as did the sorbitol. This finding again points towards a water replacement stabilization mechanism. The IgG spray-dried powder prepared from the dialyzed liquid feed showed continued substantial aggregation on dry storage at 25°C. This was substantially less in the non-dialyzed, sorbitol-containing spray-dried powder. Addition of trehalose to both dialyzed and non-dialyzed system produced substantial improvement in storage stability and reduction in aggregate formation in storage. The quantitative stabilizing effect of the trehalose was only slightly higher than that of the sorbitol. Taken together, these results indicate that both the sorbitol and trehalose stabilize the IgG primarily by a water replacement mechanism rather than by glassy immobilization. The relevance of this work is its questioning of the importance of the usually considered dominance of glassy stabilization of protein in dried systems of high glass transition temperature, such as trehalose. The low glass transition temperature sorbitol produces almost equal process and storage stability in this case.
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Salzen, E. A., & Cornell, J. M. (1968). Self-perception and species recognition in birds. Behaviour, 30(1), 44–65.
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Voss, B., Mohr, E., & Krzywanek, H. (2002). Effects of aqua-treadmill exercise on selected blood parameters and on heart-rate variability of horses. J Vet Med A Physiol Pathol Clin Med, 49(3), 137–143.
Abstract: The objectives of the present study were to investigate the effects of Aquatraining of horses (aqua-treadmill exercise; treadmill manufactured by Equitech – L.u.S. Equipment, Warendorf, Germany) on selected blood parameters [lactic acid concentration (mmol/l), haemoglobin content (g/l)] and on heart-rate variability (HRV) [heart rate (beats per min; b.p.m.), standard deviation of all NN-intervals (SDNN; ms), normalized power of the low and high frequency band (LFnorm, Hfnorm; au), % recurrence, % determinism and ratio(corr)]. Seven horses performed six exercise tests with different work loads (walking (x = 1.56 +/- 0.08 m/s) and trotting (x = 2.9 +/- 0.13 m/s): dry, water above the carpus and water above the elbow). The standardized test-protocol was: 5 min warm-up at walk while the water was pumped in, followed by the 20-min exercise period at walk or trot, followed by a 5-min walk while pumping out the water. Blood samples were taken prior to each test at rest in the stable, as well as exactly 5 min after the end of the 20-min exercise period. Electrocardiograms were recorded during rest and the 20-min exercise period. Compared to rest, neither the chosen velocities, the two water levels, nor the dry tests led to a significant increase of the lactic acid concentration in any horse. The haemoglobin content showed a significant increase as a result of exercise. Significant differences could be found between the heart rates at rest and the six exercise tests and between the mean of the levels 'walking' and the mean of the levels 'trotting'. An exercise-induced change of HRV was characterized by a decreasing SDNN, a significantly higher LFnorm (sympathetic influence) combined with a significantly lower HF(norm) power (parasympathetic activity) and a rising degree of order (significantly higher % determinism and nearly unchanged % recurrence) and stability (significantly rising ratio(corr)) of the recurrence plot. In conclusion, the used training-protocol for aqua-treadmill exercises only represents a medium-sized aerobic work load for horses, but the different levels of burden were indicated especially by changes in HRV.
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Andersson, P., Kvassman, J., Lindstrom, A., Olden, B., & Pettersson, G. (1981). Effect of NADH on the pKa of zinc-bound water in liver alcohol dehydrogenase. Eur J Biochem, 113(3), 425–433.
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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