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Biomedical subjects

E Bogin

Publications and source records attributed to E Bogin.

At least 91 records · Page 5Linked to original sources
PubMed1975

Energy-transducing membrane-bound coupling factor-ATPase from Mycobacterium phlei. I. Purification, homogeneity, and properties.

The membrane-bound coupling factor from Mycobacterium phlei was solubilized from membrane vesicles by washing with low ionic strength buffer or 0.25 M sucrose. The solubilized enzyme exhibited coupling factor, latent ATPase, and succinate oxidation-stimulating activity. Purification by affinity chromatography using Sepharose coupled to ADP yielded a homogeneous preparation of latent ATPase which was purified about 200-fold with an 84% yield in a single step. Purified latent ATPase exhibited coupling factor activity but no succinate oxidation-stimulating activity. The molecular weight of latent ATPase was determined to be 250,000 +/- 10,000 by Sephadex G-200 chromatography. The ATPase was unmasked by trypsin treatment and activated by Mg2+ ion. However, trypsin treatment inactivated the coupling factor activity in the purified enzyme, indicating that the catalytic sites for ATPase and coupling activity are different. Unlike mitochondrial ATPase, latent ATPase from M. phlei was not cold-labile. Of the nucleoside triphosphates, UTP, ITP, and epsilon-ATP (1-N6-ethenoadenosine triphosphate) were hydrolyzed to a lesser extent compared to ATP. Kinetic data showed that ADP acted as a competitive inhibitor of latent ATPase activity with a Ki of 5 x 10(-3) M. Uncouplers of oxidative phosphorylation and respiratory inhibitors did not affect the latent ATPase activity, while sodium azide (0.1 mM) inhibited the latent ATPase activity.

Adenosine Triphosphatases↗
PubMed1973

Distribution and blood-to-milk transfer of labeled antibiotics.

RADIOACTIVITY DISTRIBUTION WAS DETERMINED IN SERUM AND MILK OF LACTATING EWES AFTER PARENTERAL ADMINISTRATION OF FIVE LABELED ANTIBIOTICS: (14)C-benzylpenicillin G, (3)H-dihydrostreptomycin, (3)H-tetracycline, (14)C-chloramphenicol, and (14)C-spiramycin. Antibiotic levels were measured simultaneously by microbiological assay. Radiochemical and microbiological assay procedures presented similar kinetic patterns for uptake in serum and penetration into milk, except for tetracycline. Small reductions in milk pH markedly increased the excretion of spiramycin and slightly influenced the milk passage of penicillin, dihydrostreptomycin, and tetracycline but did not alter the transfer of chloramphenicol into milk. Thus, it appears that the five antibiotics penetrate milk in accordance with the nonionic passive diffusion principle, and that good agreement is achieved between the calculated and observed milk/serum ultrafiltrate concentration ratios obtained during equilibrium.

Animals↗
PubMed1970

Effects of heat treatment of electron-transport particles on bacterial oxidative phosphorylation.

The electron-transport particles from Mycobacterium phlei exhibit low levels of phosphorylation unless supplemented with soluble coupling proteins. Heat treatment of the electron transport particles for 15 min at 50 degrees C was found to result in a slight loss of oxidation and an activation of phosphorylation with NADH as substrate, while with succinate as substrate both activities increased. The heat-activated particles do not require the addition of soluble coupling factors and their level of oxidative phosphorylation is similar to that of the regular particles supplemented with the soluble coupling factors. In contrast to the lack of a requirement for the soluble coupling factors after heat activation, the heat-treated electron-transport particles require the presence of a particulate-bound coupling factor for phosphorylation. The heat-activated system, like the untreated system, was found to be sensitive to uncoupling agents.

Adenosine Triphosphatases↗
PubMed1969

Extraparticulate chain interaction between different electron transport particles.

Interaction or cross-linking between the respiratory chains of the electron transport particles of bacterial origin occurs with a mixture of active and inactive particles. Interaction between bacterial particles and liver sub-mitochondrial particles also occurs. Irradiation of the bacterial particles at 360 nanometers resulted in the destruction of quinone and consequent loss of ability of reduced nicotinamide adenine, dinucleotides to reduce cytochromes b, c(1), c, and a plus a(3). A mixture of both irradiated and untreated particles in the presence of the reduced dinucleotide resulted in the reduction of cytochromes c and a plus a(3), in an amount equivalent to the total concentration of these cytochromes in both types of particles. In contrast, the amount of cytochrome b reduced was equivalent to half the particle concentration or to that observed with the active particles alone. The rate of reduction of cytochromes c and a plus a(3) with the mixture of particles was similar to that with the active particles alone. The interaction or cross-linking between the particulate respiratory chains of bacteria or of bacterial and mammalian systems occurs after cytochrome b and before or at cytochrome c.

Animals↗