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PubMed1988

Determination of cytochrome b5 association reactions. Characterization of metmyoglobin and cytochrome P-450cam binding to genetically engineered cytochromeb5.

Genetically engineered cytochrome b5 has been used to quantitative binding interactions of this protein with cytochrome P-450cam and sperm whale metmyoglobin by static fluorescence titration. Two cytochrome b5 mutants were constructed by cassette mutagenesis to replace a surface threonine residue with cysteine at two crystallographically defined positions, 65 and 8, located 11 and 21 A, respectively, from the nearest heme edge. The T65C and T8C mutant proteins were labeled with the sulfhydryl selective fluorescent reagent, acrylodan, which provided a spectral probe for monitoring protein-protein association. The fluorescence emission spectra of the acrylodan-labeled T65C mutant exhibited an ionic strength-dependent, blue-shifted fluorescence enhancement upon binding met-myoglobin, cytochrome c, and cytochrome P-450cam, whereas the acrylodan-labeled T8C mutant fluorescence emission remained unchanged during all titrations. Dissociation constants of 1.3, 0.6, and 0.5 microM, pH 7.15, were measured for metmyoglobin, cytochrome P-450cam, and cytochrome c, respectively. A similar averaged binding surface for cytochrome P-450cam and cytochrome c is suggested by their closely related degree of fluorescence enhancement, degree of emission blue shift, and binding free energies. Myoglobin binds less tightly, enhances fluorescence to a greater extent, and exhibits a larger blue shift in acrylodan emission spectra suggesting a different averaged binding orientation relative to the acrylodan probe.

2-Naphthylamine↗
PubMed1987

One-electron reduction of the oxyform of 2,4-diacetyldeuterocytochrome P-450cam.

The reaction of the hydrated electron with a ferrous oxygenated form of modified cytochrome P-450cam, containing 2,4-diacetyldeuteroheme, was investigated by the use of pulse radiolysis. The ferrous oxygenated form of this enzyme was reduced by hydrated electrons to form the product, which exhibits absorption maximum at 470 and 370 nm. From the spectrum obtained, the oxidation state of the product is discussed in relation to the higher oxidation states of chloroperoxidase.

Camphor 5-Monooxygenase↗
PubMed1987

[Effect of cavinton and sulfocamphocain on systemic and cerebral hemodynamics in patients with early forms of cerebrovascular diseases].

In a study involving 33 patients with initial manifestations of inadequate cerebral blood supply and in 22 patients with transient disorders of the cerebral circulation in the presence of atherosclerosis (n = 45) and atherosclerosis with arterial hypertension (n = 8) the authors studied the effect of intravenous administration of cavinton in combination with sulfocamphocain on the clinical manifestations and on the systemic (using the method of Evans' dilution) and cerebral (using Doppler ultrasonography) hemodynamics. It has been demonstrated that both a single intravenous administration of cavinton in conjunction with sulfocamphocain and a course of treatment with these drugs reduce the volume of the circulating blood, lower the stroke and cardiac indices, increase the linear velocity of blood flow along the carotid and vertebral arteries, and decrease neurological symptomatology. The authors discuss the questions related to indications for the administration of cavinton in combination with sulfocamphocain to patients with inadequate cerebral blood supply and transient disorders of the cerebral circulation.

Camphor↗
PubMed1986

The role of arginyl residues in porphyrin binding to ferrochelatase.

The role of cationic amino acid residues in the binding of porphyrin substrates by purified bovine ferrochelatase (protoheme ferro-lyase, EC 4.99.1.1) have been examined via chemical modification with camphorquinone-10-sulfonic acid, phenylglyoxal, butanedione, and trinitrobenzene sulfonate. The data obtained show that modification of arginyl, but not lysyl, residues results in the rapid inactivation of ferrochelatase. The 2,4-disulfonate deuteroporphyrin, which is a competitive inhibitor of mammalian ferrochelatase, protects the enzyme against inactivation. Ferrous iron has no protective effect. Reaction with radiolabeled phenylglyoxal shows that modification of 1 arginyl residue causes maximum inhibition of enzyme activity. The inactivation does not follow simple pseudo-first order reaction kinetics, but is distinctly biphasic in nature. Comparison of the enzyme kinetics for modified versus unmodified enzyme show that modification with camphorquinone-10-sulfonic acid has no effect on the Km for iron but does alter the Km for porphyrin.

Amino Acids↗
PubMed1985

[Mechanisms of development and blockade of epileptic activity in the brain].

Experiments on mollusk neurons showed the presence of 3 types of neurons with different activity character and different sensitivity to convulsants. The highest sensitivity to corazol and other convulsants was characteristic of spontaneuosly active "impulse" motoneurons with the threshold dose of corazol being 1 X 10(-4) M. Intergrative neurons without background spontaneous activity were the least sensitive, with the threshold dose of corazol being 1-5 X 10(-3) M. "Impulse" cells of the mollusk were compared with epileptic neurons of the brain. It was shown that "impulse" and epileptic activity was brought about by a peculiar change in the ionic permeability of the membrane, activation of the channels of a slow ascending current, a slow growth of potassium permeability and the resultant appearance of an area of negative resistance in the volt-ampere characteristics of ionic currents of the membrane. The convulsants were capable of inducing these changes in the electrophysiological characteristics of the neuronal membrane, while classical anticonvulsants eliminated them.

Animals↗