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	Author	Steinhoff, H.J.
	Title	A continuous wave laser T-jump apparatus and its application to chemical reactions in hemoglobin single crystals			Type	Journal Article
	Year	1988	Publication	Journal of Biochemical and Biophysical Methods	Abbreviated Journal	J Biochem Biophys Methods
	Volume	15	Issue	6	Pages	319-330
	Keywords	Animals; Chemistry; Crystallization; Heat; Hemoglobins; Horses/blood; *Lasers; Methemoglobin; Solutions; Thermodynamics; Thiocyanates
	Abstract	A laser temperature jump apparatus is constructed where the T-jump is achieved by means of the direct absorption of continuous laser radiation of low intensity by a solid sample. The final temperature in the irradiated volume element is reached when the absorbed radiation power equals the dissipation of heat by heat conduction. The time range from the beginning of irradiation to the stationary state depends on the geometry of the irradiated volume element and is less than 10 ms. The heating laser beam is simultaneously used to detect the relaxation to the new chemical equilibrium in the sample. Relaxation processes with relaxation rates between 10(2) s-1 and less than 10(-3) s-1 on samples with volumes less than 10(-3) mm3 may be investigated using this T-jump method. One application of this method is the determination of reaction rates of ligand reactions in hemoglobin single crystals. Rate constants obtained for the reaction of thiocyanate with crystallized horse methemoglobin are presented.
	Address	Institut fur Biophysik, Ruhr-Universitat Bochum, F.R.G
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0165-022X	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:3379245			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3804
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	Author	Selby, L.A.; Marienfeld, C.J.; Pierce, J.O.
	Title	The effects of trace elements on human and animal health			Type	Journal Article
	Year	1970	Publication	Journal of the American Veterinary Medical Association	Abbreviated Journal	J Am Vet Med Assoc
	Volume	157	Issue	11	Pages	1800-1808
	Keywords	Anemia, Hypochromic/veterinary; Animal Nutrition Physiology; Animals; Artiodactyla/physiology; Chemistry; Cobalt/analysis/metabolism; Copper/analysis/metabolism; Deficiency Diseases/veterinary; Dogs/physiology; Ecology; Horses/physiology; Humans; Iodine/analysis/metabolism; Iron/analysis/metabolism; Manganese/analysis/metabolism; Nutritional Requirements; Selenium/metabolism; Trace Elements/metabolism; Zinc/analysis/metabolism
	Abstract
	Address
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0003-1488	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:4922190			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	2733
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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		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
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0449-3087	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:1795293			Approved	no
	Call Number	refbase @ user @			Serial	322
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	Author	Rosa, P.A.J.; Azevedo, A.M.; Aires-Barros, M.R.
	Title	Application of central composite design to the optimisation of aqueous two-phase extraction of human antibodies			Type	Journal Article
	Year	2007	Publication	Journal of Chromatography. A	Abbreviated Journal	J Chromatogr A
	Volume	1141	Issue	1	Pages	50-60
	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
	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%.
	Address	IBB Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical Engineering, Instituto Superior Tecnico, Av Rovisco Pais, 1049-001 Lisbon, Portugal
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0021-9673	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:17196214			Approved	no
	Call Number				Serial	1842
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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
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0002-7863	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:17274615			Approved	no
	Call Number				Serial	1832
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	Author	Polverini, E.; Cugini, G.; Annoni, F.; Abbruzzetti, S.; Viappiani, C.; Gensch, T.
	Title	Molten globule formation in apomyoglobin monitored by the fluorescent probe Nile Red			Type	Journal Article
	Year	2006	Publication	Biochemistry	Abbreviated Journal	Biochemistry
	Volume	45	Issue	16	Pages	5111-5121
	Keywords	Animals; Apoproteins/chemistry/metabolism; Binding Sites; Computer Simulation; Fluorescent Dyes/analysis; Horses; Hydrogen-Ion Concentration; Models, Molecular; Myoglobin/chemistry/metabolism; Oxazines/*analysis/chemistry; Protein Binding; Protein Folding; Protein Structure, Tertiary
	Abstract	The interaction of nile red (NR) with apomyoglobin (ApoMb) in the native (pH 7) and molten globule (pH 4) states was investigated using experimental and computational methods. NR binds to hydrophobic locations in ApoMb with higher affinity (K(d) = 25 +/- 5 microM) in the native state than in the molten globule state (K(d) = 52 +/- 5 microM). In the molten globule state, NR is located in a more hydrophobic environment. The dye does not bind to the holoprotein, suggesting that the binding site is located at the heme pocket. In addition to monitoring steady-state properties, the fluorescence emission of NR is capable of tracking submillisecond, time-resolved structural rearrangements of the protein, induced by a nanosecond pH jump. Molecular dynamics simulations were run on ApoMb at neutral pH and at pH 4. The structure obtained for the molten globule state is consistent with the experimentally available structural data. The docking of NR with the crystal structure shows that the ligand binds into the binding pocket of the heme group, with an orientation bringing the planar ring system of NR to overlap with the position of two of the heme porphyrin rings in Mb. The docking of NR with the ApoMb structure at pH 4 shows that the dye binds to the heme pocket with a slightly less favorable binding energy, in keeping with the experimental K(d) value. Under these conditions, NR is positioned in a different orientation, reaching a more hydrophobic environment in agreement with the spectroscopic data.
	Address	Dipartimento di Fisica, Universita degli Studi di Parma, Viale G. P. Usberti 7/A, 43100 Parma, Italy
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0006-2960	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:16618100			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	3763
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	Author	Pierce, M.M.; Nall, B.T.
	Title	Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization			Type	Journal Article
	Year	2000	Publication	Journal of Molecular Biology	Abbreviated Journal	J Mol Biol
	Volume	298	Issue	5	Pages	955-969
	Keywords	Amino Acid Sequence; Amino Acid Substitution/genetics; Binding Sites; Cytochrome c Group/chemistry/genetics/metabolism; Cytochromes c; Enzyme Stability/drug effects; Fluorescence; Guanidine/pharmacology; Heme/metabolism; Histidine/genetics/metabolism; Hydrogen-Ion Concentration; Isomerism; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation/genetics; Proline/chemistry/metabolism; Protein Conformation/drug effects; Protein Denaturation/drug effects; *Protein Folding; Protein Renaturation; Saccharomyces cerevisiae/enzymology/genetics; Sequence Alignment; Thermodynamics
	Abstract	The effect of His-heme misligation on folding has been investigated for a triple mutant of yeast iso-2 cytochrome c (N26H,H33N,H39K iso-2). The variant contains a single misligating His residue at position 26, a location at which His residues are found in several cytochrome c homologues, including horse, tuna, and yeast iso-1. The amplitude for fast phase folding exhibits a strong initial pH dependence. For GdnHCl unfolded protein at an initial pH<5, the observed refolding at final pH 6 is dominated by a fast phase (tau(2f)=20 ms, alpha(2f)=90 %) that represents folding in the absence of misligation. For unfolded protein at initial pH 6, folding at final pH 6 occurs in a fast phase of reduced amplitude (alpha(2f) approximately 20 %) but the same rate (tau(2f)=20 ms), and in two slower phases (tau(m)=6-8 seconds, alpha(m) approximately 45 %; and tau(1b)=16-20 seconds, alpha(1b) approximately 35 %). Double jump experiments show that the initial pH dependence of the folding amplitudes results from a slow pH-dependent equilibrium between fast and slow folding species present in the unfolded protein. The slow equilibrium arises from coupling of the His protonation equilibrium to His-heme misligation and proline isomerization. Specifically, Pro25 is predominantly in trans in the unligated low-pH unfolded protein, but is constrained in a non-native cis isomerization state by His26-heme misligation near neutral pH. Refolding from the misligated unfolded form proceeds slowly due to the large energetic barrier required for proline isomerization and displacement of the misligated His26-heme ligand.
	Address	Center for Biomolecular Structure, Department of Biochemistry, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78229-3900, USA
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0022-2836	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:10801361			Approved	no
	Call Number	refbase @ user @			Serial	3853
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	Author	Petter-Puchner, A.H.; Froetscher, W.; Krametter-Froetscher, R.; Lorinson, D.; Redl, H.; van Griensven, M.
	Title	The long-term neurocompatibility of human fibrin sealant and equine collagen as biomatrices in experimental spinal cord injury			Type	Journal Article
	Year	2007	Publication	Experimental and Toxicologic Pathology : Official Journal of the Gesellschaft fur Toxikologische Pathologie	Abbreviated Journal	Exp Toxicol Pathol
	Volume	58	Issue	4	Pages	237-245
	Keywords	Animals; Axotomy; Biocompatible Materials/therapeutic use; Collagen/therapeutic use; Fibrin Tissue Adhesive/therapeutic use; Horses; Humans; Immunohistochemistry; Male; Motor Activity/physiology; Nerve Regeneration/physiology; Rats; Recovery of Function; Spinal Cord/pathology/physiology; Spinal Cord Injuries/pathology/*therapy; Thoracic Vertebrae
	Abstract	INTRODUCTION: While fibrin sealant (FS) and equine collagen (EC) have been used as scaffold materials in experimental spinal cord injury (SCI), questions concerning neurocompatibility still remain. In this study, we assessed potential adverse effects, as well as functional and histological impact of FS and EC in subtotal hemisection of the thoracic spinal cord (SC) in rats. METHODS: 124 male rats were randomly assigned to four main groups (n=31): Sham (SH), Lesion only (L), fibrin sealant (GFS) and equine collagen group (GEC). SH animals received laminectomy only; all other animals underwent subtotal lateral hemisection at T9. Treatment consisted of application of FS or EC into the lesion gap in GFS and GEC, which was left empty in L. GFS, GEC, L and SH were each further divided into 4 subgroups: One subgroup, consisting of 10 rats was subjected to behavioural and reflex testing before surgery and followed up on days 1,7, 14, 21, 28 post op and then sacrificed. Haemalaun or cresyl violet (CV) was used to identify neutrophils in parasagittal cord sections which were obtained on day 1 (n=7). Sections stained for quantification of microglia/macrophages using ED-1 on day 3 (n=7), day 7 (n=7) and day 28 (n=7 out of 10). Additionally, neural filament (NF) staining was chosen to detect axonal regeneration and the length of ingrowth into FS and EC, Luxol blue for myelination, Von Willebrand factor for vascularisation, and glial fibrillary acidic protein (GFAP) staining for detection of astrocytes in glial scars on day 28. RESULTS: No adverse effects were observed in the treatment groups. Compared to L, GFS and GEC performed significantly better in the Basso, Beattie, Bresnahan (BBB) score and hopping responses. Proprioceptive placing was markedly improved in FS and EC compared to L. Axonal regrowth was found in GFS and GEC--the regrowth in the GFS was accompanied by myelination and vascularisation. Glial scarring occurred in all groups. Discussion Both biomatrices improved functional recovery compared to L and no adverse effects were perceived.
	Address	Ludwig Boltzmann Institute of Experimental and Clinical Traumatology, Donaueschingenstrasse 13, 1200-Vienna, Austria
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0940-2993	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:17118635			Approved	no
	Call Number				Serial	1852
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	Author	Permyakov, S.E.; Khokhlova, T.I.; Nazipova, A.A.; Zhadan, A.P.; Morozova-Roche, L.A.; Permyakov, E.A.
	Title	Calcium-binding and temperature induced transitions in equine lysozyme: new insights from the pCa-temperature “phase diagrams”			Type	Journal Article
	Year	2006	Publication	Proteins	Abbreviated Journal	Proteins
	Volume	65	Issue	4	Pages	984-998
	Keywords	Animals; Apoproteins/chemistry/metabolism; Binding Sites; Calcium/chemistry/metabolism; Cattle; Edetic Acid/metabolism; Horses/metabolism; Hydrogen-Ion Concentration; Lactalbumin/chemistry/metabolism; Muramidase/chemistry/metabolism; Protein Denaturation; Spectrometry, Fluorescence; Temperature; Thermodynamics; Tryptophan/chemistry/metabolism
	Abstract	The most universal approach to the studies of metal binding properties of single-site metal binding proteins, i.e., construction of a “phase diagram” in coordinates of free metal ion concentration-temperature, has been applied to equine lysozyme (EQL). EQL has one relatively strong calcium binding site and shows two thermal transitions, but only one of them is Ca(2+)-dependent. It has been found that the Ca(2+)-dependent behavior of the low temperature thermal transition (I) of EQL can be adequately described based upon the simplest four-states scheme of metal- and temperature-induced structural changes in a protein. All thermodynamic parameters of this scheme were determined experimentally and used for construction of the EQL phase diagram in the pCa-temperature space. Comparison of the phase diagram with that for alpha-lactalbumin (alpha-LA), a close homologue of lysozyme, allows visualization of the differences in thermodynamic behavior of the two proteins. The thermal stability of apo-EQL (transition I) closely resembles that for apo-alpha-LA (mid-temperature 25 degrees C), while the thermal stabilities of their Ca(2+)-bound forms are almost indistinguishable. The native state of EQL has three orders of magnitude lower affinity for Ca(2+) in comparison with alpha-LA while its thermally unfolded state (after the I transition) has about one order lower (K = 15M(-1)) affinity for calcium. Circular dichroism studies of the apo-lysozyme state after the first thermal transition show that it shares common features with the molten globule state of alpha-LA.
	Address	Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, Moscow region 142290, Russia
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	1097-0134	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:17022083			Approved	no
	Call Number				Serial	1858
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	Author	Pere, M.C.
	Title	Maternal and fetal blood levels of glucose, lactate, fructose, and insulin in the conscious pig			Type	Journal Article
	Year	1995	Publication	Journal of Animal Science	Abbreviated Journal	J. Anim Sci.
	Volume	73	Issue	10	Pages	2994-2999
	Keywords	Animals; Blood Glucose/analysis; Catheterization/methods/veterinary; Consciousness/physiology; Female; Fetal Blood/chemistry; Fructose/analysis/blood; Insulin/analysis/blood; Lactates/analysis/blood; Pregnancy; Swine/blood/physiology
	Abstract	To study nutrition and metabolism in the fetal pig, a chronic catheterization method was developed that allows blood sampling in arteries and veins, at both the umbilical and uterine sources, in the conscious, unstressed animal. A catheter was inserted in the fetal aorta through a femoral artery, and another one was introduced in the umbilical vein. A catheter was put in a femoral artery of the sow so that its end was in the abdominal aorta. A fourth catheter was placed in a uterine vein draining the fetoplacental unit studied. This procedure was applied to 18 Large White primiparous sows at 99 d of gestation. Blood samples were drawn simultaneously using the four catheters before a meal at 103 d of pregnancy, and glucose, insulin, lactate, and fructose were determinated. Glycemia was 2.5 times higher in the sow than in the fetus. The extraction coefficient of glucose by the fetus amounted to 14% of the umbilical supply. The insulin level in the fetal pig was very low ( < 5 microU/mL). Lactate and fructose seemed to originate from the placenta. Blood lactate was 2.6 times lower in the sow than in the fetus, and its extraction coefficient by the fetus amounted to 8%. Fructose in the fetal blood was 2.3 times higher than that of glucose. Fructose was not utilized by the pig fetus. The present results obtained in the fetal pig are comparable to the conclusions drawn from studies with other species.
	Address	Station de Recherches Porcines, Institut National de la Recherche Agronomique, Saint-Gilles, France
	Corporate Author				Thesis
	Publisher		Place of Publication		Editor
	Language	English	Summary Language		Original Title
	Series Editor		Series Title		Abbreviated Series Title
	Series Volume		Series Issue		Edition
	ISSN	0021-8812	ISBN		Medium
	Area		Expedition		Conference
	Notes	PMID:8617670			Approved	no
	Call Number	Equine Behaviour @ team @			Serial	2751
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