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Youket, R. J., Carnevale, J. M., Houpt, K. A., & Houpt, T. R. (1985). Humoral, hormonal and behavioral correlates of feeding in ponies: the effects of meal frequency. J. Anim Sci., 61(5), 1103–1110.
Abstract: The effect of meal frequency on body fluid, glucose, triiodothyronine (T3), heart rate and behavior was measured in 10 ponies. A simple reversal design was used in which each pony received one meal/day (1X) for 2 wk and six meals/day (6X) for 2 wk. The total intake/day was held constant. Feeding was followed by a rise in plasma levels of glucose, T3, protein and osmolality. One large meal was followed by significantly greater changes in all of the variables than was a meal one-sixth the size. Plasma T3 rose from 41 +/- 5 (SE) ng/liter before feeding to 43 +/- 5 ng/liter following a small meal, but rose significantly higher, from 39 +/- 4 to 60 +/- 10 ng/liter, following a large meal. Glucose rose from 84 +/- 3 to 109 +/- 7 mg/dl following a small meal and rose significantly higher, from 83 +/- 3 to 154 +/- 11 mg/dl, after a large meal. Plasma protein rose from 6.55 +/- .14 to 6.62 +/- .16 g/dl following a small meal and from 6.45 +/- .14 to 6.99 +/- .11 g/dl following a large meal. Osmolality rose from 227 +/- 1 mosmol/liter before to 279 +/- 1 mosmol/liter following a small meal and significantly higher from 278 +/- 2 to 285 +/- 1 mosnol/liter following a large meal. Heart rate rose from 42 beats/min in the absence of feed to 50 beats/min when food was visible to the ponies and did not rise higher when eating began. There were no significant differences in the cardiac response to one large meal and that to a small meal.(ABSTRACT TRUNCATED AT 250 WORDS)
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Rosa, P. A. J., Azevedo, A. M., & Aires-Barros, M. R. (2007). Application of central composite design to the optimisation of aqueous two-phase extraction of human antibodies. J Chromatogr A, 1141(1), 50–60.
Abstract: The partition of human antibodies in aqueous two-phase systems (ATPSs) of polyethylene glycol (PEG) and phosphate was systematically studied using first pure proteins systems and then an artificial mixture of proteins containing 1mg/ml human immunoglobulin G (IgG), 10mg/ml serum albumin and 2mg/ml myoglobin. Preliminary results obtained using pure proteins systems indicated that the PEG molecular weight and concentration, the pH value and the salts concentration had a pronounced effect on the partitioning behaviour of all proteins. For high ionic strengths and pH values higher than the isoelectric point (pI) of the contaminant proteins, IgG could be selectively recovered on the top phase. According to these results, a face centred composite design was performed in order to optimise the purification of IgG from the mixture of proteins. The optimal conditions for the isolation of IgG were observed for high concentrations of NaCl and low concentrations of both phase forming components. The best purification was achieved using an ATPS containing 8% (w/w) PEG 3350, 10% (w/w) phosphate pH 6 and 15% (w/w) NaCl. A recovery yield of 101+/-7%, a purity of 99+/-0% and a yield of native IgG of 97+/-4% were obtained. Back extraction studies of IgG to a new phosphate phase were performed and higher yields were obtained using 10% phosphate buffer at pH 6. The total extraction yield was 76% and the purity 100%.
Keywords: Analysis of Variance; Animals; Antibodies/*chemistry/*isolation & purification; Buffers; Chemical Fractionation/*methods; Horses; Humans; Hydrophobicity; Isoelectric Point; Models, Biological; Molecular Weight; Myoglobin/chemistry/isolation & purification; Osmolar Concentration; Phase Transition; Polyethylene Glycols; Serum Albumin/chemistry/isolation & purification; Sodium Chloride
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