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1.
Antibiot Khimioter ; 60(11-12): 9-14, 2015.
Article in Russian | MEDLINE | ID: mdl-27141641

ABSTRACT

Oligomycins and their complexes with lithium and zinc were shown to be less active vs. cyclosporin A in inhibition of transport proteins responsible for multiple drug resistance of lymphoid leukosis P388VR cells, while certain oligomycin complexes were tens or hundreds times more active than cyclosporin A by inhibition of transport proteins in another type of tumor cells, i.e. human larynx cancer Hep-2, that makes possible the use of the oligomycins complexes with lithium and zinc for inhibition of multiple drug resistance of certain tumor types.


Subject(s)
Antineoplastic Agents/pharmacology , Coordination Complexes/pharmacology , Drug Resistance, Neoplasm/drug effects , Lithium/chemistry , Oligomycins/pharmacology , Zinc/chemistry , Animals , Antineoplastic Agents/chemistry , Carrier Proteins/antagonists & inhibitors , Cell Line, Tumor , Coordination Complexes/chemistry , Humans , Mice , Mice, Inbred DBA , Oligomycins/chemistry
2.
Antibiot Khimioter ; 55(11-12): 11-6, 2010.
Article in Russian | MEDLINE | ID: mdl-21574419

ABSTRACT

Beauveria feline No. 7 strain was isolated from the shrewmouse wool and characterized by production of a complex of destruxins cyclodepsipeptides. The strain was shown to produce significant quatities of destruxin B and pseudodestruxin C. The destruxins were found to be able to inhibit formation of biofilms by Pseudomonas aeruginosa ATCC 27833.


Subject(s)
Beauveria/metabolism , Depsipeptides/biosynthesis , Pseudomonas aeruginosa/drug effects , Shrews/microbiology , Animals , Anti-Bacterial Agents/isolation & purification , Anti-Bacterial Agents/pharmacology , Beauveria/isolation & purification , Biofilms/drug effects , Depsipeptides/isolation & purification , Depsipeptides/pharmacology , Magnetic Resonance Spectroscopy , Mass Spectrometry , Molecular Structure
3.
FEBS Lett ; 320(1): 67-70, 1993 Mar 29.
Article in English | MEDLINE | ID: mdl-8462678

ABSTRACT

A protein has been purified from pig bone marrow which enhances the activity of exogenously added granulocyte-macrophage colony stimulating factor (GM-CSF) on mouse myelopoietic colony formation in vitro. The substance alone did not exhibit any colony stimulating activity. The active fraction was isolated from the medium of pig bone marrow suspension cultures during 20-24 h. Purification to homogeneity was then performed by subsequent HPLC and SDS-PAGE. The GM-CSF enhancing protein was identified as a 155 kDa glycoprotein.


Subject(s)
Bone Marrow/chemistry , Glycoproteins/isolation & purification , Granulocyte-Macrophage Colony-Stimulating Factor/metabolism , Animals , Blotting, Western , Bone Marrow/metabolism , Chromatography, High Pressure Liquid , Culture Media, Conditioned , Electrophoresis, Polyacrylamide Gel , Glycoproteins/metabolism , Molecular Weight , Swine
4.
Scand J Immunol ; 24(3): 237-43, 1986 Sep.
Article in English | MEDLINE | ID: mdl-3529364

ABSTRACT

Bone marrow cells produce soluble mediators with structural and functional heterogeneity. They were found to stimulate antibody production at the peak of the immune response, owing to compounds of a peptide nature (Mr 2000-1300). Active material was isolated by means of gel chromatography and electrophoresis. This material positively reacts with ninhydrin, and has maximum absorption close to 278 nm. Its antibody-stimulating activity decreased or stopped completely after treatment with proteolytic enzymes. Apart from the immunostimulating activity, bone marrow mediators have opiate-like activity. They have an analgetic effect, and interact with the opiate receptors of brain nerve cells. After a physicochemical and functional analysis, we conclude that bone marrow produces regulatory peptides that were previously unknown. We called them myelopeptides.


Subject(s)
Bone Marrow/physiology , Peptides/physiology , Analgesics/isolation & purification , Animals , Antibody Formation , Cats , Chromatography, Gel , Endorphins/isolation & purification , Female , Male , Mice , Peptide Hydrolases , Peptides/isolation & purification , Swine
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