New quaternized pyridinium derivatives of betulin: Synthesis and evaluation of membranotropic properties on liposomes, pro- and eukaryotic cells, and isolated mitochondria

2021 ◽  
pp. 109678
Author(s):  
Mikhail V. Dubinin ◽  
Alena A. Semenova ◽  
Anna I. Ilzorkina ◽  
Natalia Y. Markelova ◽  
Nikita V. Penkov ◽  
...  
Keyword(s):  
Eukaryotic Cells ◽  
Isolated Mitochondria ◽  
Derivatives Of ◽  
Membranotropic Properties

scholarly journals Localization and interconversion of tetrahydropteroylglutamates in isolated pea mitochondria

1972 ◽  
Vol 128 (1) ◽  
pp. 29-40 ◽  
Author(s):  
M. T. Clandinin ◽  
E. A. Cossins
Keyword(s):  
Amino Acids ◽  
Free Amino ◽  
Lactobacillus Casei ◽  
Sucrose Density Gradient ◽  
Mitochondrial Fraction ◽  
C1 Metabolism ◽  
Isolated Mitochondria ◽  
Feeding Experiments ◽  
Pteroylglutamic Acid ◽  
Derivatives Of

1. Mitochondria were extracted from 4-day-old pea cotyledons and purified on a sucrose density gradient. 2. Microbiological assay of the purified mitochondrial fraction with Lactobacillus casei (A.T.C.C. 7469), Streptococcus faecalis (A.T.C.C. 8043) and Pediococcus cerevisiae (A.T.C.C. 8081) revealed a discrete pool of conjugated and unconjugated derivatives of tetrahydropteroylglutamic acid. 3. Solubilization and chromatographic studies of the mitochondrial fraction demonstrated the presence of formylated and methylated derivatives, 10-formyltetrahydropteroylmonoglutamic acid, 5-formyltetrahydropteroylmonoglutamic acid and 5-formyltetrahydropteroyldiglutamic acid being the major derivatives present. 4. The principal mitochondrial pteroylglutamates were labelled when dry seeds were allowed to imbibe [2-14C]pteroylglutamic acid and 5-[methyl-14C]-methyltetrahydropteroylmonoglutamic acid. 5. The ability of isolated mitochondria to catalyse oxidation and reduction of tetrahydropteroylglutamic acid derivatives was demonstrated in feeding experiments in which [14C]formaldehyde, [3-14C]serine, sodium [14C]formate, 5-[methyl-14C]methyltetrahydropteroylmonoglutamic acid or [2-14C]-glycine served as C1 donor. In addition,14C was incorporated into free amino acids related to C1 metabolism.

Enantiomers of the Amino Acid Derivatives of Fullerene C60Possess Stereospecific Membranotropic Properties

2004 ◽  
Vol 396 (1-6) ◽  
pp. 165-167 ◽  
Author(s):  
G. N. Bogdanov ◽  
R. A. Kotel'nikova ◽  
E. S. Frog ◽  
V. N. Shtol'ko ◽  
V. S. Romanova ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Derivatives ◽  
Derivatives Of ◽  
Membranotropic Properties

Influence of water-soluble derivatives of [60]fullerene on catalytic activity of monoaminе oxidase B and their membranotropic properties

2016 ◽  
Vol 65 (3) ◽  
pp. 784-789
Author(s):  
A. V. Smolina ◽  
R. A. Kotelnikova ◽  
D. A. Poletaeva ◽  
P. A. Troshin ◽  
E. A. Khakina ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Water Soluble ◽  
Influence Of Water ◽  
Derivatives Of ◽  
Membranotropic Properties

scholarly journals Influence of polymeric derivatives of guanidine on hydrobionts

Biologija ◽  
2017 ◽  
Vol 63 (3) ◽  
Author(s):  
Andriy Lysytsya ◽  
Natalya Matvienko ◽  
Mihail Kozii ◽  
Alexander Aishpur
Keyword(s):  
Bactericidal Effect ◽  
Eukaryotic Cells ◽  
Constant Concentration ◽  
Bacteriostatic Effect ◽  
Polyhexamethylene Guanidine ◽  
Order Of Magnitude ◽  
Sublethal Doses ◽  
One Year ◽  
Derivatives Of ◽  
Test Objects

It is known that polymeric derivatives of guanidine are actively used in many countries of the world as disinfectants and antiseptics. Polyhexamethylene guanidine (PHMG) and polyhexamethylene biguanidine (PHMB) are typical representatives of this class of compounds. They show a bacteriostatic effect in concentrations from 1 mg/l (or 10–4%) or above, and a bactericidal effect from 10 mg/l (10–3%) and above. It is considered that PHMG and PHMB are not very toxic to higher organisms. This is explained by the different mechanism of drugs action on prokaryotic and eukaryotic cells. However, their safety for the fauna of freshwater hydrocenoses has not been sufficiently studied. The toxic effect of the salts of PHMG on the representatives of various types and classes of hydrobionts was studied in the experiments. It has been established that the safe concentration of PHMG in water with a one-time action on selected test objects is 0.1 mg/l (10–5%). The histological analysis of a one-year-old carp that lived in an aquarium with a constant concentration of PHMG at 0.5 mg/l for 12 days showed that concentrations of an order of magnitude smaller – 0.01 mg/l (10–6%) is absolutely safe to consider. Chronic intoxication of fish caused by sublethal doses of PHMG leads to the development of numerous disorders in the liver, kidneys, and spleen, and to the inflammation of the pancreatic islets. A comparative analysis of the toxicity of PHMG for microand macroorganisms does not allow us to state that the latter are less sensitive to this xenobiotic. So far, there are not enough convincing reasons to believe that the mechanisms of action of PHMG on pro and eukaryotic cells are fundamentally different. At the same time, the binding of PHMG molecules to suspended particles in water, organic and inorganic impurities, flocculation, and biodegradation by microorganisms leads to a rapid decrease of free active molecules of this biocide in aquatic ecosystems.

scholarly journals Membranotropic properties of the water soluble amino acid and peptide derivatives of fullerene C60

FEBS Letters ◽  
1996 ◽  
Vol 389 (2) ◽  
pp. 111-114 ◽  
Author(s):  
Raisa A. Kotelnikova ◽  
Alexander I. Kotelnikov ◽  
Guennady N. Bogdanov ◽  
Valentina S. Romanova ◽  
Elena F. Kuleshova ◽  
...  
Keyword(s):  
Amino Acid ◽  
Fullerene C60 ◽  
Water Soluble ◽  
Peptide Derivatives ◽  
Derivatives Of ◽  
Membranotropic Properties

Properties of Isolated Mitochondria of Agaricus Bisporus: Their Relationship to Dormancy and the Germination of Spores

1973 ◽  
Vol 31 ◽  
pp. 458-459
Author(s):  
K. S. McCarty ◽  
R. F. Weave ◽  
L. Kemper ◽  
F. S. Vogel
Keyword(s):  
Mitochondrial Dna ◽  
Ethidium Bromide ◽  
Microscopic Examination ◽  
Agaricus Bisporus ◽  
Osmotic Shock ◽  
Electron Microscopic Examination ◽  
Electron Microscopic ◽  
Isolated Mitochondria ◽  
Dna Strands ◽  
Cytoplasmic Ribosomes

During the prodromal stages of sporulation in the Basidiomycete, Agaricus bisporus, mitochondria accumulate in the basidial cells, zygotes, in the gill tissues prior to entry of these mitochondria, together with two haploid nuclei and cytoplasmic ribosomes, into the exospores. The mitochondria contain prominent loci of DNA [Fig. 1]. A modified Kleinschmidt spread technique1 has been used to evaluate the DNA strands from purified whole mitochondria released by osmotic shock, mitochondrial DNA purified on CsCl gradients [density = 1.698 gms/cc], and DNA purified on ethidium bromide CsCl gradients. The DNA appeared as linear strands up to 25 u in length and circular forms 2.2-5.2 u in circumference. In specimens prepared by osmotic shock, many strands of DNA are apparently attached to membrane fragments [Fig. 2]. When mitochondria were ruptured in hypotonic sucrose and then fixed in glutaraldehyde, the ribosomes were released for electron microscopic examination.

High resolution spot scan imaging of frozen, hydrated actin bundles with 400kV electrons

1992 ◽  
Vol 50 (1) ◽  
pp. 512-513
Author(s):  
J. Jakana ◽  
M.F. Schmid ◽  
P. Matsudaira ◽  
W. Chiu
Keyword(s):  
High Resolution ◽  
Binding Proteins ◽  
Actin Binding ◽  
Eukaryotic Cells ◽  
Dimensional Structure ◽  
Structural Basis ◽  
Actin Bundle ◽  
Actin Bundles ◽  
3 Dimensional ◽  
Macromolecular Assembly

Actin is a protein found in all eukaryotic cells. In its polymerized form, the cells use it for motility, cytokinesis and for cytoskeletal support. An example of this latter class is the actin bundle in the acrosomal process from the Limulus sperm. The different functions actin performs seem to arise from its interaction with the actin binding proteins. A 3-dimensional structure of this macromolecular assembly is essential to provide a structural basis for understanding this interaction in relationship to its development and functions.

Structure of clathrin cages and coats in ice

1986 ◽  
Vol 44 ◽  
pp. 94-97
Author(s):  
G.P.A. Vigers ◽  
R.A. Crowther ◽  
B.M.F. Pearse
Keyword(s):  
Electron Microscopy ◽  
Heavy Chain ◽  
Outer Part ◽  
Coated Vesicles ◽  
Eukaryotic Cells ◽  
Coat Proteins ◽  
Terminal Domain ◽  
Clathrin Heavy Chain ◽  
Membrane Components

Clathrin forms the polyhedral cage of coated vesicles, which mediate the transfer of selected membrane components within eukaryotic cells. Clathrin cages and coated vesicles have been extensively studied by electron microscopy of negatively stained preparations and shadowed specimens. From these studies the gross morphology of the outer part of the polyhedral coat has been established and some features of the packing of clathrin trimers into the coat have also been described. However these previous studies have not revealed any internal details about the position of the terminal domain of the clathrin heavy chain, the location of the 100kd-50kd accessory coat proteins or the interactions of the coat with the enclosed membrane.

The Hierarchic Order of Intermediate Filament Structure and Assembly

1985 ◽  
Vol 43 ◽  
pp. 722-725
Author(s):  
U. Aebi ◽  
E.C. Glavaris ◽  
R. Eichner
Keyword(s):  
Tissue Specificity ◽  
Structural Model ◽  
Eukaryotic Cells ◽  
Cdna Sequencing ◽  
Filament Structure ◽  
Keratin Filaments ◽  
Isoelectric Points ◽  
Immunological Crossreactivity

Five different classes of intermediate-sized filaments (IFs) have been identified in differentiated eukaryotic cells: vimentin in mesenchymal cells, desmin in muscle cells, neurofilaments in nerve cells, glial filaments in glial cells and keratin filaments in epithelial cells. Despite their tissue specificity, all IFs share several common attributes, including immunological crossreactivity, similar morphology (e.g. about 10 nm diameter - hence ‘10-nm filaments’) and the ability to reassemble in vitro from denatured subunits into filaments virtually indistinguishable from those observed in vivo. Further more, despite their proteinchemical heterogeneity (their MWs range from 40 kDa to 200 kDa and their isoelectric points from about 5 to 8), protein and cDNA sequencing of several IF polypeptides (for refs, see 1,2) have provided the framework for a common structural model of all IF subunits.

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