Biomedical subjects

I V Mesyanzhinova

Publications and source records attributed to I V Mesyanzhinova.

4 recordsLinked to original sources

PubMed1990

The F1-type ATPase in anaerobic Lactobacillus casei.

An ATPase from anaerobic Lactobacillus casei has been isolated and 100-times purified. The 400 kDa enzyme molecule was found to have a hexagonal structure 10 nm in diameter composed of at least six protein masses. SDS-electrophoresis reveals four or, under certain conditions, five types of subunit, of apparent molecular masses 57 (alpha), 55 (beta), 40 (gamma), 22 (delta) and 14 (epsilon) kDa with stoichiometry of 3 alpha, 3 beta, gamma, delta, epsilon. The following features resembling F1-ATPases from other sources were found to be inherent in the solubilized L. casei ATPase. (i) Detachment from the membrane desensitizes ATPase to low DCCD concentrations and sensitizes it to water-soluble carbodiimide. (ii) Soluble ATPase is inhibited by Nbf chloride and azide, is resistant to SH-modifiers and is activated by sulfite and octyl glucoside, the activating effect being much stronger than in the case of the membrane-bound ATPase. Substrate specificity of the enzyme is also similar to that of other factors F1. Divalent cations strongly activate the soluble enzyme when added at a concentration equal to that of ATP. An excess of Mn2+, Mg2+ or Co2+ inhibits ATPase activity of F1, whereas that of Ca2+ induces its further activation. No other F1-like ATPases are found in L. casei. It is concluded that this anaerobic bacterium possesses a typical F1-ATPase similar to those in mitochondria, chloroplasts, aerobic and photosynthetic eubacteria.

Catalysis↗

PubMed1989

Structure of the ATP-synthase studied by electron microscopy and image processing.

The structure of ATP synthase from beef heart mitochondria has been studied by electron microscopy and image processing using negatively stained specimens of detergent-solubilized and membrane-bound molecules. The F1-ATPase and the membrane-embedded F0 sector of ATP synthase are found to be connected by a narrow stalk, 4-4.5 nm long and 3-3.5 nm wide, projecting about 4.2 nm from the membrane surface. The F0 sector has a globular shape, 6-8 nm in diameter and, in part, extends from the membrane lipid bilayer.

Animals↗

PubMed1987

Electron-microscopic studies on location of SH-groups in mitochondrial F1-ATPase using a ferritin label.

A new approach has been suggested for electron-microscopic study of the structure of mitochondrial F1-ATPase based on ferritin labeling. By means of sequential treatment with 2-iminothiolane and Nbs2 we obtained a modified ferritin (NbsSPrCNH-Ft) able to react with SH-groups of proteins and to form conjugates in which the protein and ferritin are bound by disulfide bonds. An electron-microscopic investigation of the negatively stained preparations of mitochondrial F1-ATPase, preincubated with modified ferritin, revealed such enzyme-ferritin conjugates. In case of modified ferritin, containing 360 mol SH-groups per mol protein, and F1-ATPase, pretreated with N-ethylmaleimide and then with dithiothreitol, conjugates were obtained in which ferritin molecules are bound to several (as many as four) of the six protein masses, comprising a bilayer molecule of the enzyme. Taking into consideration the biochemical data on the location of accessible SH-groups (only in alpha, gamma or epsilon subunits), it is inferred from the results obtained that one of the protein masses is a complex between beta subunit and at least one of the minor subunits located partially on the molecule's external side. This indicates the nonequivalence of different copies of the major subunits. Averaged images of the particles of the F1-F0 complex from bovine heart mitochondria and bacteria Micrococcus lysodeicticus were obtained. It was found that F0 component is bound to two adjacent protein masses of the F1-ATPase molecule. It is suggested that this binding may be due the nonequivalency of single-type major subunits.

Animals↗

PubMed1984

Electron microscopy of beef heart mitochondrial F1-ATPase.

The quaternary structure of isolated and membrane-bound F1-ATPase (submitochondrial particles) has been studied by electron microscopy. A model of the molecule has been proposed: six protein masses are arranged in two layers approximately at the vertices of a triangular antiprism. Computer averaging of the images showed that the frontal view of the molecule can be approximately characterized by mirror plane symmetry.

Animals↗