| Records |
| Author |
Hinchcliff, K.W.; Kohn, C.W.; Geor, R.; McCutcheon, L.J.; Foreman, J.; Andrews, F.M.; Allen, A.K.; White, S.L.; Williamson, L.H.; Maykuth, P.L. |
| Title |
Acid:base and serum biochemistry changes in horses competing at a modified 1 Star 3-day-event |
Type |
Journal Article |
| Year |
1995 |
Publication |
Equine Veterinary Journal. Supplement |
Abbreviated Journal |
Equine Vet J Suppl |
| Volume |
|
Issue |
20 |
Pages |
105-110 |
Keywords  |
*Acid-Base Equilibrium; Animals; Blood Proteins/analysis; Body Water/metabolism; Carbon Dioxide/blood; Electrolytes/*blood; Female; Hematocrit/veterinary; Homeostasis; Horses/*blood/physiology; Hydrogen-Ion Concentration; Male; Physical Conditioning, Animal/*physiology |
| Abstract |
We examined the effects of participation in each of 3 modifications of Day 2 of a 3-day-event on blood and serum variables indicative of hydration, acid:base status and electrolyte homeostasis of horses. Three groups of horses – 8 European (E) horses and 2 groups each of 9 North American horses performed identical Days 1 (dressage) and 3 (stadium jumping) of a 3-day-event. E horses and one group of the North American horses (TD) performed modifications of Day 2 of a 1 Star 3-day-event and the other group of North American horses (HT) performed a Horse Trial on Day 2. Jugular venous blood was collected from each horse on the morning of Day 2 before any warm-up activity, between 4 min 55 s and 5 min 15 s after Phase D and the following morning. Eight E horses, 5 TD horses and 8 HT horses completed the trials. There were few significant differences in acid:base or serum biochemistry variables detected among horses performing either 2 variations of the Speed and Endurance day of a 1 Star 3-day-event, or a conventional Horse Trial. Failure to detect differences among groups may have been related to the low statistical power associated with the small number of horses, especially in the TD group, variation in quality of horses among groups and the different times of the day at which the E horses competed. Differences detected among time points were usually common to all groups and demonstrated metabolic acidosis with a compensatory respiratory alkalosis, a reduction in total body water and cation content, and hypocalcaemia. Importantly, horses of all groups did not replenish cation, chloride, and calcium deficits after 14-18 h of recovery. |
| Address |
Department of Veterinary Clinical Sciences, College of Veterinary Medicine, Ohio State University, Columbus 43210-1089, USA |
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Thesis |
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Place of Publication |
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Editor |
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| Language |
English |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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ISBN |
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Medium |
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Expedition |
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Conference |
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| Notes |
PMID:8933092 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3740 |
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| Author |
Dunn, M.F.; Branlant, G. |
| Title |
Roles of zinc ion and reduced coenzyme in horse liver alcohol dehydrogenase catalysis. The mechanism of aldehyde activation |
Type |
Journal Article |
| Year |
1975 |
Publication |
Biochemistry |
Abbreviated Journal |
Biochemistry |
| Volume |
14 |
Issue |
14 |
Pages |
3176-3182 |
| Keywords |
*Alcohol Oxidoreductases/metabolism; Aldehydes/*pharmacology; Animals; Binding Sites; Enzyme Activation/drug effects; Horses; Hydrogen-Ion Concentration; Kinetics; Liver/enzymology; *NAD/analogs & derivatives/pharmacology; Oxidation-Reduction; Protein Binding; Spectrophotometry; Spectrophotometry, Ultraviolet; Temperature; *Zinc/pharmacology |
| Abstract |
1,4,5,6-Tetrahydronicotinamide adenine dinucleotide (H2NADH) has been investigated as a reduced coenzyme analog in the reaction between trans-4-N,N-dimethylaminocinnamaldehyde (I) (lambdamax 398 nm, epsilonmax 3.15 X 10-4 M-minus 1 cm-minus 1) and the horse liver alcohol dehydrogenase-NADH complex. These equilibrium binding and temperature-jump kinetic studies establish the following. (i) Substitution of H2NADH for NADH limits reaction to the reversible formation of a new chromophoric species, lambdamax 468 nm, epsilonmax 5.8 x 10-4 M-minus 1 cm-minus 1. This chromophore is demonstrated to be structurally analogous to the transient intermediate formed during the reaction of I with the enzyme-NADH complex [Dunn, M. F., and Hutchison, J. S. (1973), Biochemistry 12, 4882]. (ii) The process of intermediate formation with the enzyme-NADH complex is independent of pH over the range 6.13-10.54. Although studies were limited to the pH range 5.98-8.72, a similar pH independence appears to hold for the H2NADH system. (iii) Within the ternary complex, I is bound within van der Waal's contact distance of the coenzyme nicotinamide ring. (iv) Formation of the transient intermediate does not involve covalent modification of coenzyme. Based on these findings, we conclude that zinc ion has a Lewis acid function in facilitating the chemical activation of the aldehyde carbonyl for reduction, and that reduced coenzyme plays a noncovalent effector role in this substrate activating step. |
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Thesis |
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Place of Publication |
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Editor |
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| Language |
English |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0006-2960 |
ISBN |
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Medium |
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Expedition |
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Conference |
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| Notes |
PMID:238585 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3817 |
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| Author |
Jablonska, E.M.; Ziolkowska, S.M.; Gill, J.; Szykula, R.; Faff, J. |
| Title |
Changes in some haematological and metabolic indices in young horses during the first year of jump-training |
Type |
Journal Article |
| Year |
1991 |
Publication |
Equine Veterinary Journal |
Abbreviated Journal |
Equine Vet J |
| Volume |
23 |
Issue |
4 |
Pages |
309-311 |
| Keywords |
Alanine Transaminase/blood; Animals; Bicarbonates/blood; Blood Glucose/analysis; Blood Proteins/analysis; Breeding; Carbon Dioxide/blood; Exercise Test/veterinary; Fatty Acids, Nonesterified/blood; Female; Fructose-Bisphosphate Aldolase/blood; Hematocrit/veterinary; Hemoglobins/analysis; Horses/*blood/metabolism; Hydrogen-Ion Concentration; Lactates/blood; Male; Oxygen/blood; *Physical Conditioning, Animal; Pyruvates/blood |
| Abstract |
Effects of an 18 min exercise test, on three separate occasions during a one year jump-training programme, was studied in seven horses. Determinations were carried out on venous blood for packed cell volume, haemoglobin, total protein, lactate and pyruvate, glucose, free fatty acids, insulin, glucagon, blood gases, bicarbonate, pH, aldolase, aspartate aminotransferase and alanine amino-transferase. Exercise caused a slight increase in lactate and pyruvate, total protein, aldolase, alanine aminotransferase, pO2, bicarbonate and pH. Glucose, free fatty acids and pCO2 levels decreased. Training caused no significant difference in these changes. However, during the year, increases in lactate and decreases in pH (resting levels) were observed. |
| Address |
Department of Vertebrate Animal Physiology, Warszawa, Poland |
| Corporate Author |
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Thesis |
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Place of Publication |
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Editor |
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| Language |
English |
Summary Language |
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Original Title |
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| Series Editor |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
0425-1644 |
ISBN |
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Medium |
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| Area |
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Expedition |
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Conference |
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| Notes |
PMID:1915234 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3801 |
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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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Thesis |
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| Publisher |
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Place of Publication |
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Editor |
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| Language |
English |
Summary Language |
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Original Title |
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| Series Editor |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
0014-2956 |
ISBN |
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Medium |
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| Area |
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Expedition |
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Conference |
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| Notes |
PMID:7011796 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3810 |
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| Author |
Czerlinski, G.H.; Erickson, J.O.; Theorell, H. |
| Title |
Chemical relaxation studies on the horse liver alcohol dehydrogenase system |
Type |
Journal Article |
| Year |
1979 |
Publication |
Physiological Chemistry and Physics |
Abbreviated Journal |
Physiol Chem Phys |
| Volume |
11 |
Issue |
6 |
Pages |
537-569 |
| Keywords |
Alcohol Oxidoreductases/*metabolism; Animals; Buffers; Electron Transport; Ethanol/metabolism; Horses; Hydrogen-Ion Concentration; Liver/*enzymology; Mathematics; NAD/metabolism; Oscillometry; Osmolar Concentration; Temperature; Time Factors |
| Abstract |
Chemical relaxation studies on the system horse liver alcohol dehydrogenase, nicotinamide adenine dinucleotide, and ethanol were conducted observing fluorescence changes between 400 and 500 nm. Temperature-jump experiments were performed at pH 6.5, 7.0, 8.0, and 9.0; concentration-jump experiments at pH 9.0. The reciprocal of the slowest relaxation time was found to be linearly dependent upon the enzyme concentration for relatively low enzyme concentrations, as predicted earlier. Use of the wide pH-range necessitated expression of the four apparent dissociation constants of the catalytic reaction cycle in terms of pH-independent constants. The system was described in terms of only one (or two) catalysis-linked protons not associated with the electron transfer. Protonic steps in a buffered system are in rapid equilibrium, too fast to be measured with the equipment available. Assuming only two of the four bimolecular reaction steps in the four-step cycle are fast compared to the remaining two, six cases may be considered with six expressions for the reciprocal of the slowest relaxation time. Comparison with the experimental data revealed that the bimolecular reaction steps governing the slowest relaxation time change with pH. Above the effective time resolution of the temperature-lump instrument with fluorescence detection (0.1 msec) only one other relaxation time was detectable and only at pH 9. This relaxation time, found to be independent of the concentration of all reactants within experimental error (r = 10 +/- 5 msec), is most likely due to an interconversion among ternary complexes. |
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Thesis |
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Place of Publication |
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Editor |
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English |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
0031-9325 |
ISBN |
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Medium |
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| Area |
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Expedition |
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Conference |
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| Notes |
PMID:44918 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3813 |
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| Author |
Czerlinski, G.H.; Wagner, M.; Erickson, J.O.; Theorell, H. |
| Title |
Chemical relaxation studies on the system liver alcohol dehydrogenase, NADH and imidazole |
Type |
Journal Article |
| Year |
1975 |
Publication |
Acta Chemica Scandinavica. Series B: Organic Chemistry and Biochemistry |
Abbreviated Journal |
Acta Chem Scand B |
| Volume |
29 |
Issue |
8 |
Pages |
797-810 |
| Keywords |
Alcohol Oxidoreductases/*metabolism; Animals; Computers; Hydrogen-Ion Concentration; Imidazoles/*metabolism; Kinetics; Liver/enzymology/*metabolism; Mathematics; Models, Chemical; NAD/*metabolism; Time Factors |
| Abstract |
Several years ago, Theorell and Czerlinski conducted experiments on the system of horse liver alcohol dehydrogenase, reduced nicotinamide adenine dinucleotide and imidazole, using the first version of the temperature jump apparatus with detection of changes in fluorescence. These early experiments were repeated with improved instrumentation and confirmed the early experiments in general terms. However, the improved detection system allowed to measure a slight concentration dependence of the relaxation time of around 3 ms. Furthermore, the chemical relaxation time was smaller than the one determined earlier (by factor 2). The data were evaluated much more rigorously than before, allowing an appropriate interpretation of the results. The observed relaxation time is largely due to rate constants in an interconversion of ternary complexes, which are faster than three (of the four) dissociation rate constants, determined previously by Theorell and McKinley-McKee.1,2 This fact contributed to earlier difficulties of finding any concentration dependence. However, the binding of imidazole to the binary enzyme-coenzyme complex can be made to couple kinetically into the interconversion rate of the two ternary complexes. The observed signal derives largely from the ternary complex(es). A substantial fluorescence signal change is associated with the observed relaxation process, suggesting a relocation of the imidazole in reference to the nicotinamide moiety of the bound coenzyme. Nine models are considered with two types of coupling of pre-equilibria (none-all). Quantitative evaluations favor the model with two ternary complexes connected by an interconversion outside the four-step (bimolecular) cycle. The ternary complex outside the cycle has much higher fluorescence yield than the one inside. The interconversion equilibrium is near unity for imidazole. If it would be shifted very much to the side of the “dead-end” complex (as in isobutyramide?!), stimulating action could not take place. |
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Thesis |
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Place of Publication |
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Editor |
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| Language |
English |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
0302-4369 |
ISBN |
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Medium |
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| Area |
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Expedition |
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Conference |
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| Notes |
PMID:882 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
3887 |
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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 |
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Thesis |
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Place of Publication |
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Editor |
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English |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0022-2836 |
ISBN |
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Medium |
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Expedition |
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Conference |
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| Notes |
PMID:10801361 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
3853 |
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| Author |
Saigo, S. |
| Title |
Kinetic and equilibrium studies of alkaline isomerization of vertebrate cytochromes c |
Type |
Journal Article |
| Year |
1981 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
| Volume |
669 |
Issue |
1 |
Pages |
13-20 |
| Keywords |
Amino Acid Sequence; Animals; Cytochrome c Group/*metabolism; Dogs; Hydrogen-Ion Concentration; Isomerism; Kinetics; Vertebrates/metabolism |
| Abstract |
Equilibria and kinetics of alkaline isomerization of seven ferricytochromes c from vertebrates were studied by pH-titration and pH-jump methods in the pH region of 7-12. In the equilibrium behavior, no significant difference was detected among the cytochromes c, whereas marked differences in the kinetic behavior were observed. According to the kinetic behavior of the isomerization, the cytochromes c examined fall into three classes: Group I (horse, sheep, dog and pigeon cytochromes c), Group II (tuna and bonito cytochromes c) and Group III (rhesus monkey cytochrome c). The kinetic results are interpreted in terms of the sequential scheme: Neutral form in equilibrium with fast Transient form in equilibrium with slow Alkaline form where the neutral and alkaline forms are the species stable at neutral and alkaline pH, respectively, and the transient form is a kinetic intermediate. From comparison of the primary sequences of the seven cytochromes c and the classification of these cytochromes c, it is concluded that the amino acid substitution Phe/Tyr at the 46-th position has a major influence on the kinetic behavior. In Group II and III cytochromes c, the ionization of Tyr-46 is suggested to bring about loosening of the heme crevice and thus facilitate the ligand replacement involved in the isomerization. |
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Thesis |
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Place of Publication |
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Editor |
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English |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0006-3002 |
ISBN |
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Medium |
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Expedition |
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Conference |
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| Notes |
PMID:6271238 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
3871 |
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| Author |
Hirota, S.; Suzuki, M.; Watanabe, Y. |
| Title |
Hydrophobic effect of trityrosine on heme ligand exchange during folding of cytochrome c |
Type |
Journal Article |
| Year |
2004 |
Publication |
Biochemical and Biophysical Research Communications |
Abbreviated Journal |
Biochem Biophys Res Commun |
| Volume |
314 |
Issue |
2 |
Pages |
452-458 |
| Keywords |
Amino Acids/chemistry; Animals; Cytochromes c/*chemistry; Heme/*chemistry; Histidine/chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium/chemistry; Peptides/chemistry; Protein Folding; Spectrophotometry; Spectrum Analysis, Raman; Tyrosine/*analogs & derivatives/*chemistry |
| Abstract |
Effect of a hydrophobic peptide on folding of oxidized cytochrome c (cyt c) is studied with trityrosine. Folding of cyt c was initiated by pH jump from 2.3 (acid-unfolded) to 4.2 (folded). The Soret band of the 2-ms transient absorption spectrum during folding decreased its intensity and red-shifted from 397 to 400 nm by interaction with trityrosine, whereas tyrosinol caused no significant effect. The change in the transient absorption spectrum by interaction with trityrosine was similar to that obtained with 100 mM imidazole, which showed that the population of the intermediate His/His coordinated species increased during folding of cyt c by interaction with trityrosine. The absorption change was biphasic, the fast phase (82+/-9s(-1)) corresponding to the transition from the His/H(2)O to the His/Met coordinated species, whereas the slow phase (24+/-3s(-1)) from His/His to His/Met. By addition of trityrosine, the relative ratio of the slow phase increased, due to increase of the His/His species at the initial stage of folding. According to the resonance Raman spectra of cyt c, the high-spin 6-coordinate and low-spin 6-coordinate species were dominated at pH 2.3 and 4.2, respectively, and these species were not affected by addition of trityrosine. These results demonstrated that the His/His species increased by interaction with trityrosine at the initial stage of cyt c folding, whereas the heme coordination structure was not affected by trityrosine when the protein was completely unfolded or folded. Hydrophobic peptides thus may be useful to study the effects of hydrophobic interactions on protein folding. |
| Address |
Department of Physical Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, 607-8414 Kyoto, Japan. hirota@mb.kyoto-phu.ac.jp |
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Place of Publication |
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English |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0006-291X |
ISBN |
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Medium |
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Expedition |
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Conference |
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| Notes |
PMID:14733927 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3777 |
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| Author |
Hillidge, C.J.; Lees, P. |
| Title |
Cardiac output in the conscious and anaesthetised horse |
Type |
Journal Article |
| Year |
1975 |
Publication |
Equine veterinary journal |
Abbreviated Journal |
Equine Vet J |
| Volume |
7 |
Issue |
1 |
Pages |
16-21 |
| Keywords |
Anesthesia, Inhalation/*veterinary; Animals; Carbon Dioxide/blood; *Cardiac Output/veterinary; *Consciousness; Electrocardiography/veterinary; Ether, Ethyl; Female; Halothane; Heart Rate; Heart Ventricles/physiology; Horses/*physiology; Hydrogen-Ion Concentration; Male; Oxygen/blood; Posture |
| Abstract |
Cardiac output in the horse was measured before and at predetermined times during 2-hour periods of thiopentone-halothane and thiopentone-diethyl ether anaesthesia. Left ventricular stroke volume was decreased to a similar extent during anaesthesia with each volatile agent, but a greater reduction in cardiac output occurred during halothane anaesthesia. This finding reflected the differing effects of halothane and ether on heart rate, a slight bradycardia occurring with the former agent while ether produced a small degree of tachycardia. The latter effect was attributed to enhanced sympathoadrenal activity. Changes in cardiac output and stroke volume were considered in relation to other factors, including arterial blood pH and tensions of oxygen and carbon dioxide. Positive correlations between some of these variables and cardiac function were established. With both volatile agents the reductions in stroke volume and cardiac output were related to the duration of anaesthesia, being greatest during the early stages. Possible reasons for the tendency of stroke volume and cardiac output to return towards control levels are discussed. |
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Thesis |
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Place of Publication |
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Editor |
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English |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
0425-1644 |
ISBN |
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Medium |
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| Area |
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Expedition |
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Conference |
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| Notes |
PMID:234842 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
102 |
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