Records |
Author |
Abbruzzetti, S.; Crema, E.; Masino, L.; Vecli, A.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. |
Title |
Fast events in protein folding: structural volume changes accompanying the early events in the N-->I transition of apomyoglobin induced by ultrafast pH jump |
Type |
Journal Article |
Year |
2000 |
Publication |
Biophysical Journal |
Abbreviated Journal |
Biophys J |
Volume |
78 |
Issue |
1 |
Pages |
405-415 |
Keywords |
Animals; Apoproteins/*chemistry; Horses; *Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Myoglobin/*chemistry; Protein Conformation; *Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence |
Abstract |
Ultrafast, laser-induced pH jump with time-resolved photoacoustic detection has been used to investigate the early protonation steps leading to the formation of the compact acid intermediate (I) of apomyoglobin (ApoMb). When ApoMb is in its native state (N) at pH 7.0, rapid acidification induced by a laser pulse leads to two parallel protonation processes. One reaction can be attributed to the binding of protons to the imidazole rings of His24 and His119. Reaction with imidazole leads to an unusually large contraction of -82 +/- 3 ml/mol, an enthalpy change of 8 +/- 1 kcal/mol, and an apparent bimolecular rate constant of (0.77 +/- 0.03) x 10(10) M(-1) s(-1). Our experiments evidence a rate-limiting step for this process at high ApoMb concentrations, characterized by a value of (0. 60 +/- 0.07) x 10(6) s(-1). The second protonation reaction at pH 7. 0 can be attributed to neutralization of carboxylate groups and is accompanied by an apparent expansion of 3.4 +/- 0.2 ml/mol, occurring with an apparent bimolecular rate constant of (1.25 +/- 0.02) x 10(11) M(-1) s(-1), and a reaction enthalpy of about 2 kcal/mol. The activation energy for the processes associated with the protonation of His24 and His119 is 16.2 +/- 0.9 kcal/mol, whereas that for the neutralization of carboxylates is 9.2 +/- 0.9 kcal/mol. At pH 4.5 ApoMb is in a partially unfolded state (I) and rapid acidification experiments evidence only the process assigned to carboxylate protonation. The unusually large contraction and the high energetic barrier observed at pH 7.0 for the protonation of the His residues suggests that the formation of the compact acid intermediate involves a rate-limiting step after protonation. |
Address |
Dipartimento di Fisica, Universita di Parma, 43100 Parma, Italia |
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English |
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0006-3495 |
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PMID:10620304 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
3792 |
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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 |
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ISSN |
1097-0134 |
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PMID:17022083 |
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no |
Call Number |
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Serial |
1858 |
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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 |
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English |
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0940-2993 |
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PMID:17118635 |
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no |
Call Number |
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Serial |
1852 |
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Author |
Boucher, J.M.; Hanosset, R.; Augot, D.; Bart, J.M.; Morand, M.; Piarroux, R.; Pozet-Bouhier, F.; Losson, B.; Cliquet, F. |
Title |
Detection of Echinococcus multilocularis in wild boars in France using PCR techniques against larval form |
Type |
Journal Article |
Year |
2005 |
Publication |
Veterinary Parasitology |
Abbreviated Journal |
Vet Parasitol |
Volume |
129 |
Issue |
3-4 |
Pages |
259-266 |
Keywords |
Animals; Base Sequence; DNA, Helminth/chemistry/genetics; Echinococcosis/parasitology/pathology/*veterinary; Echinococcus multilocularis/*isolation & purification; Electron Transport Complex IV/chemistry/genetics; France; Histocytochemistry/veterinary; Liver/parasitology/pathology; Male; Molecular Sequence Data; Polymerase Chain Reaction/veterinary; Sequence Alignment; Sus scrofa/*parasitology; Swine Diseases/*parasitology/pathology |
Abstract |
Recently, new data have been collected on the distribution and ecology of Echinococcus multilocularis in European countries. Different ungulates species such as pig, goat, sheep, cattle and horse are known to host incomplete development of larval E. multilocularis. We report a case of E. multilocularis portage in two wild boars from a high endemic area in France (Department of Jura). Histological examination was performed and the DNA was isolated from hepatic lesions then amplified by using three PCR methods in two distinct institutes. Molecular characterisation of PCR products revealed 99% nucleotide sequence homology with the specific sequence of the U1 sn RNA gene of E. multilocularis, 99 and 99.9% nucleotide sequence homology with the specific sequence of the cytochrome oxydase gene of Echinococcus genus and 99.9% nucleotide sequence homology with a genomic DNA sequence of Echinococcus genus for the first and the second wild boar, respectively. |
Address |
AFSSA Nancy, Laboratoire d'Etudes et de Recherches sur la Rage et la Pathologie des Animaux Sauvages, Domaine de Pixerecourt-B.P. 9, Malzeville F 54220, France |
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English |
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ISSN |
0304-4017 |
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PMID:15845281 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
2629 |
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Author |
Griffin, B. |
Title |
The use of fecal markers to facilitate sample collection in group-housed cats |
Type |
Journal Article |
Year |
2002 |
Publication |
Contemporary Topics in Laboratory Animal Science / American Association for Laboratory Animal Science |
Abbreviated Journal |
Contemp Top Lab Anim Sci |
Volume |
41 |
Issue |
2 |
Pages |
51-56 |
Keywords |
Animals; Behavior, Animal; Biological Markers/*analysis; Cats/*physiology/psychology; Diet/veterinary; Feces/*chemistry; Food Coloring Agents/analysis; Housing, Animal; Individuality; Plastics/analysis; Specimen Handling/methods/*veterinary |
Abstract |
The provision of proper social housing is a priority when designing an experiment using domestic cats as laboratory animals. When animals are group-housed, studies requiring analysis of stool samples from individual subjects pose difficulty in sample collection and identification. In this study, commercially available concentrated food colorings (known as bakers pastes) were used as fecal markers in group-housed cats. Cats readily consumed 0.5 ml of bakers paste food coloring once daily in canned cat food. Colorings served as fecal markers by imparting a distinct color to each cat s feces, allowing identification in the litter box. In addition, colored glitter (1/8 teaspoon in canned food) was fed to cats and found to be a reliable fecal marker. Long-term feeding of colorings and glitter was found to be safe and effective at yielding readily identifiable stools. |
Address |
Scott-Ritchey Research Center, College of Veterinary Medicine, Auburn University, Alabama 36841, USA |
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English |
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Edition |
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ISSN |
1060-0558 |
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Notes |
PMID:11958604 |
Approved |
no |
Call Number |
Equine Behaviour @ team @ |
Serial |
4165 |
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Author |
Touma, C.; Palme, R. |
Title |
Measuring fecal glucocorticoid metabolites in mammals and birds: the importance of validation |
Type |
Journal Article |
Year |
2005 |
Publication |
Annals of the New York Academy of Sciences |
Abbreviated Journal |
Ann N Y Acad Sci |
Volume |
1046 |
Issue |
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Pages |
54-74 |
Keywords |
Animals; Birds/*metabolism; Circadian Rhythm; Feces/*chemistry; Glucocorticoids/*analysis; Mammals/*metabolism; Reproducibility of Results; Seasons; Sex Factors |
Abstract |
In recent years, the noninvasive monitoring of steroid hormone metabolites in feces of mammals and droppings of birds has become an increasingly popular technique. It offers several advantages and has been applied to a variety of species under various settings. However, using this technique to reliably assess an animal's adrenocortical activity is not that simple and straightforward to apply. Because clear differences regarding the metabolism and excretion of glucocorticoid metabolites (GCMs) exist, a careful validation for each species and sex investigated is obligatory. In this review, general analytical issues regarding sample storage, extraction procedures, and immunoassays are briefly discussed, but the main focus lies on experiments and recommendations addressing the validation of fecal GCM measurements in mammals and birds. The crucial importance of scrutinizing the physiological and biological validity of fecal GCM analyses in a given species is stressed. In particular, the relevance of the technique to detect biologically meaningful alterations in adrenocortical activity must be shown. Furthermore, significant effects of the animals' sex, the time of day, season, and different life history stages are discussed, bringing about the necessity to seriously consider possible sex differences as well as diurnal and seasonal variations. Thus, comprehensive information on the animals' biology and stress physiology should be carefully taken into account. Together with an extensive physiological and biological validation, this will ensure that the measurement of fecal GCMs can be used as a powerful tool to assess adrenocortical activity in diverse investigations on laboratory, companion, farm, zoo, and wild animals. |
Address |
Max Planck Institute of Psychiatry, Department of Behavioral Neuroendocrinology, Kraepelinstrasse 2-10, D-80804 Munich, Germany. touma@mpipsykl.mpg.de |
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ISSN |
0077-8923 |
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PMID:16055843 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
4073 |
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Author |
Mostl, E.; Rettenbacher, S.; Palme, R. |
Title |
Measurement of corticosterone metabolites in birds' droppings: an analytical approach |
Type |
Journal Article |
Year |
2005 |
Publication |
Annals of the New York Academy of Sciences |
Abbreviated Journal |
Ann N Y Acad Sci |
Volume |
1046 |
Issue |
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Pages |
17-34 |
Keywords |
Animals; Birds/*metabolism; Corticosterone/*analysis/metabolism; Feces/*chemistry; Gas Chromatography-Mass Spectrometry; Immunoassay; Molecular Structure; Reproducibility of Results; Sensitivity and Specificity |
Abstract |
Fecal steroid analyses are becoming increasingly popular among both field and laboratory scientists. The benefits associated with sampling procedures that do not require restraint, anesthesia, and blood collection include less risk to subject and investigator, as well as the potential to obtain endocrine profiles that are not influenced by the sampling procedure itself. In the feces, a species-specific pattern of metabolites is present, because glucocorticoids are extensively metabolized. Therefore, selection of adequate extraction procedures and immunoassays for measuring the relevant metabolites is a serious issue. In this review, emphasis is placed on the establishment and analytical validation of methods to measure glucocorticoid metabolites for a noninvasive evaluation of adrenocortical activity in droppings of birds. |
Address |
Institute of Biochemistry, Department of Natural Sciences, University of Veterinary Medicine, Vienna, Veterinarplatz 1, A-1210 Vienna, Austria. erich.moestl@vu-wien.ac.at |
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0077-8923 |
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PMID:16055841 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
4082 |
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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 |
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0021-8812 |
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PMID:8617670 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
2751 |
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Author |
McCutcheon, L.J.; Geor, R.J. |
Title |
Influence of training on sweating responses during submaximal exercise in horses |
Type |
Journal Article |
Year |
2000 |
Publication |
Journal of Applied Physiology (Bethesda, Md. : 1985) |
Abbreviated Journal |
J Appl Physiol |
Volume |
89 |
Issue |
6 |
Pages |
2463-2471 |
Keywords |
Animals; Body Fluids/metabolism; Body Temperature; Body Weight; Environment; Female; Horses/*physiology; Ions; Male; Motor Activity/*physiology; Oxygen Consumption; Physical Conditioning, Animal/*physiology; Sweat/chemistry; Sweating/*physiology; Time Factors |
Abstract |
Sweating responses were examined in five horses during a standardized exercise test (SET) in hot conditions (32-34 degrees C, 45-55% relative humidity) during 8 wk of exercise training (5 days/wk) in moderate conditions (19-21 degrees C, 45-55% relative humidity). SETs consisting of 7 km at 50% maximal O(2) consumption, determined 1 wk before training day (TD) 0, were completed on a treadmill set at a 6 degrees incline on TD0, 14, 28, 42, and 56. Mean maximal O(2) consumption, measured 2 days before each SET, increased 19% [TD0 to 42: 135 +/- 5 (SE) to 161 +/- 4 ml. kg(-1). min(-1)]. Peak sweating rate (SR) during exercise increased on TD14, 28, 42, and 56 compared with TD0, whereas SRs and sweat losses in recovery decreased by TD28. By TD56, end-exercise rectal and pulmonary artery temperature decreased by 0.9 +/- 0.1 and 1.2 +/- 0.1 degrees C, respectively, and mean change in body mass during the SET decreased by 23% (TD0: 10.1 +/- 0.9; TD56: 7.7 +/- 0.3 kg). Sweat Na(+) concentration during exercise decreased, whereas sweat K(+) concentration increased, and values for Cl(-) concentration in sweat were unchanged. Moderate-intensity training in cool conditions resulted in a 1.6-fold increase in sweating sensitivity evident by 4 wk and a 0.7 +/- 0.1 degrees C decrease in sweating threshold after 8 wk during exercise in hot, dry conditions. Altered sweating responses contributed to improved heat dissipation during exercise and a lower end-exercise core temperature. Despite higher SRs for a given core temperature during exercise, decreases in recovery SRs result in an overall reduction in sweat fluid losses but no change in total sweat ion losses after training. |
Address |
Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ontario, Canada N1G 2W1. jmccutch@uoguelph.ca |
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ISSN |
8750-7587 |
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PMID:11090603 |
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no |
Call Number |
refbase @ user @ |
Serial |
1922 |
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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 |
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English |
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Edition |
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ISSN |
0165-022X |
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PMID:3379245 |
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no |
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Equine Behaviour @ team @ |
Serial |
3804 |
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