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Dyson, H. J., & Beattie, J. K. (1982). Spin state and unfolding equilibria of ferricytochrome c in acidic solutions. J Biol Chem, 257(5), 2267–2273.
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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Saigo, S. (1981). A transient spin-state change during alkaline isomerization of ferricytochrome c. J Biochem (Tokyo), 89(6), 1977–1980.
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.
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Ridge, J. A., Baldwin, R. L., & Labhardt, A. M. (1981). Nature of the fast and slow refolding reactions of iron(III) cytochrome c. Biochemistry, 20(6), 1622–1630.
Abstract: The fast and slow refolding reactions of iron(III) cytochrome c (Fe(III) cyt c), previously studied by Ikai et al. (Ikai, A., Fish, W. W., & Tanford, C. (1973) J. Mol. Biol. 73, 165--184), have been reinvestigated. The fast reaction has the major amplitude (78%) and is 100-fold faster than the slow reaction in these conditions (pH 7.2, 25 degrees C, 1.75 M guanidine hydrochloride). We show here that native cyt c is the product formed in the fast reaction as well as in the slow reaction. Two probes have been used to test for formation of native cyt c. absorbance in the 695-nm band and rate of reduction of by L-ascorbate. Different unfolded species (UF, US) give rise to the fast and slow refolding reactions, as shown both by refolding assays at different times after unfolding (“double-jump” experiments) and by the formation of native cyt c in each of the fast and slow refolding reactions. Thus the fast refolding reaction is UF leads to N and the slow refolding reaction is Us leads to N, where N is native cyt c, and there is a US in equilibrium UF equilibrium in unfolded cyt c. The results are consistent with the UF in equilibrium US reaction being proline isomerization, but this has not yet been tested in detail. Folding intermediates have been detected in both reactions. In the UF leads to N reaction, the Soret absorbance change precedes the recovery of the native 695-nm band spectrum, showing that Soret absorbance monitors the formation of a folding intermediate. In the US leads to N reaction an ascorbate-reducible intermediate has been found at an early stage in folding and the Soret absorbance change occurs together with the change at 695 nm as N is formed in the final stage of folding.
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Tumova, B. (1980). Equine influenza--a segment in influenza virus ecology. Comp Immunol Microbiol Infect Dis, 3(1-2), 45–59.
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Milouchine, V. N. (1980). The role of WHO in international studies on the ecology of influenza in animals. Comp Immunol Microbiol Infect Dis, 3(1-2), 25–31.
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Tobin, T., & Combie, J. D. (1982). Performance testing in horses: a review of the role of simple behavioral models in the design of performance experiments. J Vet Pharmacol Ther, 5(2), 105–118.
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Alexander, F., Horner, M. W., & Moss, M. S. (1967). The salivary secretion and clearance in the horse of chloral hydrate and its metabolites. Biochem Pharmacol, 16(7), 1305–1311.
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Washino, R. K., & Tempelis, C. H. (1967). Host-feeding patterns of Anopheles freeborni in the Sacramento Valley, California. J Med Entomol, 4(3), 311–314.
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Alexander, F. (1966). A study of parotid salivation in the horse. J Physiol, 184(3), 646–656.
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Holbrook, A. A. (1969). Biology of equine piroplasmosis. J Am Vet Med Assoc, 155(2), 453–454.
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