| Records |
| Author |
Rodier, F. |
| Title |
[Spectral properties of porcine plasminogen: study of the acidic transition (author's transl)] |
Type |
Journal Article |
| Year |
1976 |
Publication |
European journal of biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
| Volume |
63 |
Issue |
2 |
Pages |
553-562 |
| Keywords |
Animals; Binding Sites; Guanidines; Hydrogen-Ion Concentration; *Plasminogen; Protein Binding; Protein Conformation; Spectrometry, Fluorescence; Spectrophotometry; Spectrophotometry, Ultraviolet; Swine; Temperature |
| Abstract |
The acidic transition of porcine plasminogen, prepared by affinity chromatography, was studied by non-destructive methods. These methods are based on the analysis of the behaviour of the tryptophyls under various conditions. The perturbation of the absorption and emission spectra by pH or temperature and the dynamic quenching of the intrinsic fluorescence are used to obtain information on structural changes which affect the environment of these residues. It is shown that by decreasing pH the fluorescence emission spectra are shifted toward the long wavelengths, with a broadening of the fluorescence band. The same effect can be obtained at constant pH by heating the protein solution. In order to analyze these phenomena, it is assumed that the fluorescence intensities at 355 nm and 328 nm reflect the proportion of the tryptophans which are exposed to the solvent, and buried, respectively. The plot of the ratio of the fluorescence intensities at these wavelengths versus pH or temperature leads to a titration curve showing an unmasking of tryptophans. The proportion of exposed tryptophans is measured by the dynamic fluorescence quenching technique and the data analyzed according to Lehrer. The plot of the fraction of exposed tryptophyls versus pH also shows the unmasking of these chromophores. Thermal perturbation of a solution of plaminogen at neutral pH induces a difference absorption spectrum whose amplitudes at the maxima are proportional to the number of exposed aromatic residues. The comparison with a solution of fully denatured plasminogen in 6 M guanidium chloride, where all the tryptophyls are exposed, shows that the percentage of exposure is equal to 59%. This number is significantly higher than the percentage found by the fluorescence quenching technique (20%), indicating that some tryptophyls are located in crevices, exposed to the solvent but not to the iodide. At acidic pH the absorption difference spectra induced by thermal perturbation are not classical, since they show an inversion and a new band between 300 nm and 305 nm. This band is mentioned in the literature as a minor band of tryptophan which appears when this chromophore is located in an asymmetric environment. On plotting the maximum amplitude of these spectra obtained at acidic pH versus temperature, we obtain a curve indicating that two types of antagonistic interactions are involved in the perturbation of the chromophores spectra. The spectrophotometric titration of plasminogen gives classical absorption difference spectra. By plotting the maximum amplitude at 292 nm versus pH, we obtain a titration curve with an apparent pK of 2.9 units. This pK is acidic which respect to the pK value of a normal carboxyl. This low value can be due to a positively charged group in the neighbourhood of a carboxyl, which interacts with one or more chromophores. When the carboxyl becomes protonated, this positively charged group is free and available to perturb the environment of some chromophores... |
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| Language |
French |
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Original Title |
Proprietes spectrales du plasminogene porcin. Etude de la transition acide |
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0014-2956 |
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| Notes |
PMID:4326 |
Approved |
no |
| Call Number |
Admin @ knut @ |
Serial |
22 |
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| Author |
Crowell-Davis, S.L.; Houpt, K.A.; Carnevale, J. |
| Title |
Feeding and drinking behavior of mares and foals with free access to pasture and water |
Type |
Journal Article |
| Year |
1985 |
Publication |
Journal of animal science |
Abbreviated Journal |
J. Anim Sci. |
| Volume |
60 |
Issue |
4 |
Pages |
883-889 |
| Keywords |
Animals; *Drinking Behavior; *Feeding Behavior; Female; Horses/*physiology; Male; Poaceae; Seasons; Temperature; Time Factors |
| Abstract |
The feeding and drinking behavior of 11 mares and 15 foals living on pasture with free access to water was recorded during 2,340 15-min focal samples taken over 2 yr. Lactating mares on pasture spent about 70% of the day feeding. Foals began feeding on their first day of life. As they grew older, they spent progressively more time feeding, but still spent only 47 +/- 6% of the time feeding by 21 wk of age. Foals fed primarily during the early morning and evening. While grass formed the major proportion of the diet of both foals and mares, they also ate clay, humus, feces, bark, leaves and twigs. Almost all feeding by foals was done while their mothers were feeding. Movement to water sources was frequently, but not invariably, carried out by an entire herd. Frequency (P = .005) but not duration (P greater than .05) of drinking bouts by mares increased as the temperature increased. Frequency was greatest at 30 to 35 C, at which temperature mares drank once every 1.8 h. Frequency of drinking varied with the time of day (P less than .01), being rarest during the early morning (0500 to 0900 h eastern daylight time) and most frequent during the afternoon (1300 to 1700 h). Drinking by foals was very rare. The youngest age at which a foal was observed to drink was 3 wk, and 8 of 15 foals were never observed to drink before weaning. |
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English |
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0021-8812 |
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| Notes |
PMID:3988655 |
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no |
| Call Number |
refbase @ user @ |
Serial |
54 |
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| Author |
Chmel, L.; Hasilikova, A.; Hrasko, J.; Vlacilikova, A. |
| Title |
The influence of some ecological factors on keratinophilic fungi in the soil |
Type |
Journal Article |
| Year |
1972 |
Publication |
Sabouraudia |
Abbreviated Journal |
Sabouraudia |
| Volume |
10 |
Issue |
1 |
Pages |
26-34 |
| Keywords |
Animals; Arthrodermataceae/growth & development/isolation & purification/metabolism; Carbohydrates; Czechoslovakia; Ecology; Fungi/growth & development/*isolation & purification/metabolism; Hair; Horses; Humic Substances; Humidity; Keratins/metabolism; Microsporum/isolation & purification; Mitosporic Fungi/isolation & purification; Phosphates; Seasons; Soil; *Soil Microbiology; Species Specificity; Temperature; Trichophyton/isolation & purification |
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English |
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0036-2174 |
ISBN |
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| Notes |
PMID:5063162 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
2719 |
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| Author |
Gilmanshin, R.; Callender, R.H.; Dyer, R.B. |
| Title |
The core of apomyoglobin E-form folds at the diffusion limit |
Type |
Journal Article |
| Year |
1998 |
Publication |
Nature Structural Biology |
Abbreviated Journal |
Nat Struct Biol |
| Volume |
5 |
Issue |
5 |
Pages |
363-365 |
| Keywords |
Animals; Apoproteins/*chemistry; Diffusion; Horses; Myoglobin/*chemistry; *Protein Folding; Spectroscopy, Fourier Transform Infrared; Temperature |
| Abstract |
The E-form of apomyoglobin has been characterized using infrared and fluorescence spectroscopies, revealing a compact core with native like contacts, most probably consisting of 15-20 residues of the A, G and H helices of apomyoglobin. Fast temperature-jump, time-resolved infrared measurements reveal that the core is formed within 96 micros at 46 degrees C, close to the diffusion limit for loop formation. Remarkably, the folding pathway of the E-form is such that the formation of a limited number of native-like contacts is not rate limiting, or that the contacts form on the same time scale expected for diffusion controlled loop formation. |
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English |
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1072-8368 |
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| Notes |
PMID:9586997 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3795 |
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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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English |
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Edition |
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0021-9258 |
ISBN |
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| Notes |
PMID:6277891 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3807 |
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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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English |
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Abbreviated Series Title |
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Edition |
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| ISSN |
0031-9325 |
ISBN |
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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 |
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. |
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English |
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Series Issue |
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Edition |
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0014-2956 |
ISBN |
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| Notes |
PMID:20304 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3814 |
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| Author |
Bayley, P.; Martin, S.; Anson, M. |
| Title |
Temperature-jump circular dichroism: observation of chiroptical relaxation processes at millisecond time resolution |
Type |
Journal Article |
| Year |
1975 |
Publication |
Biochemical and Biophysical Research Communications |
Abbreviated Journal |
Biochem Biophys Res Commun |
| Volume |
66 |
Issue |
1 |
Pages |
303-308 |
| Keywords |
*Alcohol Oxidoreductases/metabolism; Animals; Circular Dichroism; Horses; Kinetics; Liver/enzymology; Mathematics; Protein Conformation; Temperature; Time Factors |
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English |
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0006-291X |
ISBN |
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| Notes |
PMID:1172440 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3816 |
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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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Edition |
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0006-2960 |
ISBN |
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| Notes |
PMID:238585 |
Approved |
no |
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Equine Behaviour @ team @ |
Serial |
3817 |
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| Author |
Cho, K.C.; Chan, K.K. |
| Title |
Kinetics of cold-induced denaturation of metmyoglobin |
Type |
Journal Article |
| Year |
1984 |
Publication |
Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology |
Abbreviated Journal |
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| Volume |
786 |
Issue |
1-2 |
Pages |
103-108 |
| Keywords |
Metmyoglobin denaturation; Temperature jump; Denaturation kinetics; Conformational transformation; (Horse heart) |
| Abstract |
Using a slow temperature-jump spectrophotometer, we have studied the kinetics of cold-induced denaturation of metmyoglobin between 0[degree sign]C and 20[degree sign]C at acidic pH. The time-scale of the transition is slow and is of the order of minutes. The results are consistent with the transition's involving a total of three states, native (N), transient intermediate (I) and denatured (D), which are converted from one to the other in that order. |
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no |
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refbase @ user @ |
Serial |
3978 |
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