| |
Records |
Links |
|
Author |
Jallon, J.M.; Risler, Y.; Iwatsubo, M. |
|
| |
Title |
Beef liver L-Glutamate dehydrogenase mechanism: presteady state study of the catalytic reduction of 2.oxoglutarate by NADPH |
Type |
Journal Article |
| |
Year |
1975 |
Publication |
Biochemical and biophysical research communications |
Abbreviated Journal |
Biochem Biophys Res Commun |
|
| |
Volume |
67 |
Issue |
4 |
Pages |
1527-1536 |
|
| |
Keywords |
Animals; Cattle; Glutamate Dehydrogenase/*metabolism; Ketoglutaric Acids; Kinetics; Liver/*enzymology; Nadp; Oxidation-Reduction; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet |
|
| |
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 |
0006-291X |
ISBN |
|
Medium |
|
|
| |
Area |
|
Expedition |
|
Conference |
|
|
| |
Notes |
PMID:1038 |
Approved |
no |
|
| |
Call Number |
Admin @ knut @ |
Serial |
21 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Bykov, S.; Lednev, I.; Ianoul, A.; Mikhonin, A.; Munro, C.; Asher, S.A. |
|
| |
Title |
Steady-state and transient ultraviolet resonance Raman spectrometer for the 193-270 nm spectral region |
Type |
Journal Article |
| |
Year |
2005 |
Publication |
Applied Spectroscopy |
Abbreviated Journal |
Appl Spectrosc |
|
| |
Volume |
59 |
Issue |
12 |
Pages |
1541-1552 |
|
| |
Keywords |
Animals; Equipment Design; Equipment Failure Analysis; Horses; Kinetics; Metmyoglobin/*analysis; Myocardium/*metabolism; Reproducibility of Results; Sensitivity and Specificity; Spectrophotometry, Ultraviolet/*instrumentation/methods; Spectrum Analysis, Raman/*instrumentation/methods |
|
| |
Abstract |
We describe a state-of-the-art tunable ultraviolet (UV) Raman spectrometer for the 193-270 nm spectral region. This instrument allows for steady-state and transient UV Raman measurements. We utilize a 5 kHz Ti-sapphire continuously tunable laser (approximately 20 ns pulse width) between 193 nm and 240 nm for steady-state measurements. For transient Raman measurements we utilize one Coherent Infinity YAG laser to generate nanosecond infrared (IR) pump laser pulses to generate a temperature jump (T-jump) and a second Coherent Infinity YAG laser that is frequency tripled and Raman shifted into the deep UV (204 nm) for transient UV Raman excitation. Numerous other UV excitation frequencies can be utilized for selective excitation of chromophoric groups for transient Raman measurements. We constructed a subtractive dispersion double monochromator to minimize stray light. We utilize a new charge-coupled device (CCD) camera that responds efficiently to UV light, as opposed to the previous CCD and photodiode detectors, which required intensifiers for detecting UV light. For the T-jump measurements we use a second camera to simultaneously acquire the Raman spectra of the water stretching bands (2500-4000 cm(-1)) whose band-shape and frequency report the sample temperature. |
|
| |
Address |
Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, 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 |
0003-7028 |
ISBN |
|
Medium |
|
|
| |
Area |
|
Expedition |
|
Conference |
|
|
| |
Notes |
PMID:16390595 |
Approved |
no |
|
| |
Call Number |
Equine Behaviour @ team @ |
Serial |
3767 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Abbruzzetti, S.; Viappiani, C.; Sinibaldi, F.; Santucci, R. |
|
| |
Title |
Kinetics of histidine dissociation from the heme Fe(III) in N-fragment (residues 1-56) of cytochrome c |
Type |
Journal Article |
| |
Year |
2004 |
Publication |
The Protein Journal |
Abbreviated Journal |
Protein J |
|
| |
Volume |
23 |
Issue |
8 |
Pages |
519-527 |
|
| |
Keywords |
Animals; Cytochromes c/*chemistry; Enzyme Activation; Histidine/*chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Lasers; Ligands; Peptide Mapping; Photolysis; Spectrophotometry |
|
| |
Abstract |
We have here investigated the dissociation kinetics of the His side chains axially ligated to the heme-iron in the ferric (1-56 residues) N-fragment of horse cyt c. The ligand deligation induced by acidic pH-jump occurs as a biexponential process with different pre-exponential factors, consistent with a structural heterogeneity in solution and the presence of two differently coordinated species. In analogy with GuHCl-denatured cyt c, our data indicate the presence in solution of two ferric forms of the N-fragment characterized by bis-His coordination, as summarized in the following scheme: His18-Fe(III)-His26 <==> His18-Fe(III)-His33. We have found that the pre-exponential factors depend on the extent of the pH-jump. This may be correlated with the different pKa values shown by His26 and His33; due to steric factors, His26 binds to the heme-Fe(III) less strongly than His33, as recently shown by studies on denatured cyt c. Interestingly, the two lifetimes are affected by temperature but not by the extent of the pH-jump. The lower pKa for the deligation reaction required the use of an improved laser pH-jump setup, capable of inducing changes in H+ concentration as large as 1 mM after the end of the laser pulse. For the ferric N-fragment, close activation entropy values have been determined for the two histidines coordinated to the iron; this result significantly differs from that for GuHCl-denatured cyt c, where largely different values of activation entropy were calculated. This underlines the role played by the missing segment (residues 57-104) peptide chain in discriminating deligation of the “nonnative” His from the sixth coordination position of the metal. |
|
| |
Address |
Dipartimento di Fisica, Universita degli Studi di Parma, Parco Area delle Scienze 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 |
1572-3887 |
ISBN |
|
Medium |
|
|
| |
Area |
|
Expedition |
|
Conference |
|
|
| |
Notes |
PMID:15648974 |
Approved |
no |
|
| |
Call Number |
Equine Behaviour @ team @ |
Serial |
3770 |
|
| Permanent link to this record |
| |
|
| |
|
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 |
|
| |
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 |
0006-291X |
ISBN |
|
Medium |
|
|
| |
Area |
|
Expedition |
|
Conference |
|
|
| |
Notes |
PMID:14733927 |
Approved |
no |
|
| |
Call Number |
Equine Behaviour @ team @ |
Serial |
3777 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Ballew, R.M.; Sabelko, J.; Gruebele, M. |
|
| |
Title |
Direct observation of fast protein folding: the initial collapse of apomyoglobin |
Type |
Journal Article |
| |
Year |
1996 |
Publication |
Proceedings of the National Academy of Sciences of the United States of America |
Abbreviated Journal |
Proc. Natl. Acad. Sci. U.S.A. |
|
| |
Volume |
93 |
Issue |
12 |
Pages |
5759-5764 |
|
| |
Keywords |
Animals; Apoproteins/*chemistry; Circular Dichroism; Horses; Kinetics; Muscle, Skeletal/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Infrared; Temperature |
|
| |
Abstract |
The rapid refolding dynamics of apomyoglobin are followed by a new temperature-jump fluorescence technique on a 15-ns to 0.5-ms time scale in vitro. The apparatus measures the protein-folding history in a single sweep in standard aqueous buffers. The earliest steps during folding to a compact state are observed and are complete in under 20 micros. Experiments on mutants and consideration of steady-state CD and fluorescence spectra indicate that the observed microsecond phase monitors assembly of an A x (H x G) helix subunit. Measurements at different viscosities indicate diffusive behavior even at low viscosities, in agreement with motions of a solvent-exposed protein during the initial collapse. |
|
| |
Address |
School of Chemical Sciences and Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana, 61801, 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 |
0027-8424 |
ISBN |
|
Medium |
|
|
| |
Area |
|
Expedition |
|
Conference |
|
|
| |
Notes |
PMID:8650166 |
Approved |
no |
|
| |
Call Number |
Equine Behaviour @ team @ |
Serial |
3798 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Chiba, K.; Ikai, A.; Kawamura-Konishi, Y.; Kihara, H. |
|
| |
Title |
Kinetic study on myoglobin refolding monitored by five optical probe stopped-flow methods |
Type |
Journal Article |
| |
Year |
1994 |
Publication |
Proteins |
Abbreviated Journal |
Proteins |
|
| |
Volume |
19 |
Issue |
2 |
Pages |
110-119 |
|
| |
Keywords |
Animals; Chromatography, Gel; Circular Dichroism; Horses; Kinetics; Metmyoglobin/analogs & derivatives/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Urea |
|
| |
Abstract |
The refolding kinetics of horse cyanometmyoglobin induced by concentration jump of urea was investigated by five optical probe stopped-flow methods: absorption at 422 nm, tryptophyl fluorescence at around 340 nm, circular dichroism (CD) at 222 nm, CD at 260 nm, and CD at 422 nm. In the refolding process, we detected three phases with rate constants of > 1 x 10(2) s-1, (4.5-9.3) s-1, and (2-5) x 10(-3) s-1. In the fastest phase, a substantial amount of secondary structure (approximately 40%) is formed within the dead time of the CD stopped-flow apparatus (10.7 ms). The kinetic intermediate populated in the fastest phase is shown to capture a hemindicyanide, suggesting that a “heme pocket precursor” recognized by hemindicyanide must be constructed within the dead time. In the middle phase, most of secondary and tertiary structures, especially around the captured hemindicyanide, have been constructed. In the slowest phase, we detected a minor structural rearrangement accompanying the ligand-exchange reaction in the fifth coordination of ferric iron. We present a possible model for the refolding process of myoglobin in the presence of the heme group. |
|
| |
Address |
Laboratory of Biodynamics, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Kanagawa, Japan |
|
| |
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 |
0887-3585 |
ISBN |
|
Medium |
|
|
| |
Area |
|
Expedition |
|
Conference |
|
|
| |
Notes |
PMID:8090705 |
Approved |
no |
|
| |
Call Number |
Equine Behaviour @ team @ |
Serial |
3799 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Dyson, H.J.; Beattie, J.K. |
|
| |
Title |
Spin state and unfolding equilibria of ferricytochrome c in acidic solutions |
Type |
Journal Article |
| |
Year |
1982 |
Publication |
The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
|
| |
Volume |
257 |
Issue |
5 |
Pages |
2267-2273 |
|
| |
Keywords |
Animals; *Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium; Protein Binding; Protein Conformation; Spectrophotometry; Temperature |
|
| |
Abstract |
Equilibrium, stopped flow, and temperature-jump spectrophotometry have been used to identify processes in the unfolding of ferricytochrome c in acidic aqueous solutions. A relaxation occurring in approximately 100 microseconds involves perturbation of a spin-equilibrium between two folded conformers of the protein with methionine-80 coordinated or dissociated from the heme iron. The protein unfolds more slowly, in milliseconds, with dissociation and protonation of histidine-18. These two transitions appear cooperative in equilibrium measurements at low (0.01 M) ionic strength, but are separated at higher (0.10 M) ionic strength. They are resolved under both conditions in the dynamic measurements. The spin-equilibrium description permits a unified explanation of a number of properties of ferricytochrome c in acidic aqueous solutions. |
|
| |
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 |
0021-9258 |
ISBN |
|
Medium |
|
|
| |
Area |
|
Expedition |
|
Conference |
|
|
| |
Notes |
PMID:6277891 |
Approved |
no |
|
| |
Call Number |
Equine Behaviour @ team @ |
Serial |
3807 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Saigo, S. |
|
| |
Title |
A transient spin-state change during alkaline isomerization of ferricytochrome c |
Type |
Journal Article |
| |
Year |
1981 |
Publication |
Journal of Biochemistry |
Abbreviated Journal |
J Biochem (Tokyo) |
|
| |
Volume |
89 |
Issue |
6 |
Pages |
1977-1980 |
|
| |
Keywords |
Animals; *Cytochrome c Group; Horses; Hydrogen-Ion Concentration; Isomerism; Kinetics; Myocardium/enzymology; Oxidation-Reduction; Spectrophotometry |
|
| |
Abstract |
Kinetic difference spectra during the alkaline isomerization of ferricytochrome c were obtained by the pH-jump method in the range of 540 to 655 nm. The spectrum of the transient intermediate, which appears during the course of the isomerization, was reproduced from the spectra. The intermediate showed an intense absorption band at 600 nm, indicating that it is a high spin or mixed spin species. This is in contrast to the stable neutral and alkaline forms which are low spin species. The transient spin-state change during the isomerization was also observed upon rapid oxidation of ferrocytochrome c at alkaline pH. |
|
| |
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 |
0021-924X |
ISBN |
|
Medium |
|
|
| |
Area |
|
Expedition |
|
Conference |
|
|
| |
Notes |
PMID:6270075 |
Approved |
no |
|
| |
Call Number |
Equine Behaviour @ team @ |
Serial |
3808 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Wilson, M.T.; Ranson, R.J.; Masiakowski, P.; Czarnecka, E.; Brunori, M. |
|
| |
Title |
A kinetic study of the pH-dependent properties of the ferric undecapeptide of cytochrome c (microperoxidase) |
Type |
Journal Article |
| |
Year |
1977 |
Publication |
European Journal of Biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
|
| |
Volume |
77 |
Issue |
1 |
Pages |
193-199 |
|
| |
Keywords |
Animals; Cyanides; *Cytochrome c Group/metabolism; Ferric Compounds; Horses; Hydrogen-Ion Concentration; Imidazoles; Kinetics; Mathematics; Myocardium/enzymology; *Oligopeptides/metabolism; *Peptide Fragments/metabolism; Protein Binding; Spectrophotometry; Temperature |
|
| |
Abstract |
The ferric form of the haem undecapeptide, derived from horse cytochrome c by peptic digestion, undergoes at least three pH-induced transitions with pK values of 3.4, 5.8 and 7.6. Temperature-jump experiments suggest that the first of these is due to the binding of a deprotonated imidazole group to the feric iron while the second and third arise from the binding of the two available amino groups present (the alpha-NH2 of valine and the epsilon-NH2 of lysine). Molecular models indicate that steric retraints on the peptide dictate that these amino groups may only coordinate to iron atoms via intermolecular bonds, thus leading to the polymerization of the peptide. Cyanide binding studies are in agreement with these conclusions and also yield a value of 3.6 X 10(6) M-1 s-1 for the intrinsic combination constant of CN- anion with the haem. A model is proposed which describes the pH-dependent properties of the ferric undecapeptide. |
|
| |
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 |
0014-2956 |
ISBN |
|
Medium |
|
|
| |
Area |
|
Expedition |
|
Conference |
|
|
| |
Notes |
PMID:20304 |
Approved |
no |
|
| |
Call Number |
Equine Behaviour @ team @ |
Serial |
3814 |
|
| Permanent link to this record |
| |
|
| |
|
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. |
|
| |
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 |
0006-2960 |
ISBN |
|
Medium |
|
|
| |
Area |
|
Expedition |
|
Conference |
|
|
| |
Notes |
PMID:238585 |
Approved |
no |
|
| |
Call Number |
Equine Behaviour @ team @ |
Serial |
3817 |
|
| Permanent link to this record |
