| Records |
| Author |
Hertsch, B.; Becker, C. |
| Title |
[Occurrence of aseptic necrosis of the palmar and plantar ligament in the horse--a contribution to the differentiation of sesamoid bone diseases] |
Type |
Journal Article |
| Year |
1986 |
Publication |
DTW. Deutsche tierarztliche Wochenschrift |
Abbreviated Journal |
Dtsch Tierarztl Wochenschr |
| Volume |
93 |
Issue |
6 |
Pages |
263-266 |
| Keywords |
Animals; Diagnosis, Differential; Horse Diseases/*pathology; Horses; Ligaments, Articular/*pathology; Osteonecrosis/*pathology; Sesamoid Bones/*pathology |
| Abstract |
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Place of Publication |
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Editor |
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| Language |
German |
Summary Language |
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Original Title |
Zum Vorkommen der aseptischen Nekrose im Ligamentum palmare bzw. plantare beim Pferd--ein Beitrag zur Differenzierung der Gleichbeinerkrankungen |
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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 |
0341-6593 |
ISBN |
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Expedition |
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Conference |
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Notes  |
PMID:3527654 |
Approved |
no |
| Call Number |
refbase @ user @ |
Serial |
150 |
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| 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. |
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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 |
0021-9258 |
ISBN |
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Medium |
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Expedition |
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Conference |
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| Notes |
PMID:6277891 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3807 |
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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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| 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 |
0014-2956 |
ISBN |
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Medium |
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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 |
| Permanent link to this record |
