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LABORATORY OF MOLECULAR ENZYMOLOGY
HEAD:
Jean I. Akopian, DrSc, Professor,
Corr. member of NAS RA
E-mail: jeanakopian@gmail.com
Phone(off): +374 10 228-015
Phone(cell): +374 91 422-668
Laboratory members:
General information:
The laboratory studies physical-chemical and catalytic properties of enzymes and the molecular mechanisms of regulation of their activity.
The separation of enzyme's subunits was achieved by the method of affine modification on the homogeneous preparations of creatine kinase (CK) from rabbit
muscle and their functional non-identity was shown, also amino acid residues of the enzyme's active center, that are responsible for catalysis were identified.
The activating and inhibitory effects of organic compounds of molybdenum and tungsten, as well as various phospholipid compounds were shown on highly purified
preparations of CK from human myocardium. Based on the similarity of complex compounds and components of the lipid membranes it was concluded on the possibility
of sensing enzyme sites designed to interact with the surface of membranes (with their help). The structure and organization of repeats adjacent to the
gene of bovine growth hormone were studied. The transcription process has asymmetrical nature. The plasmid spectrum of spore-forming bacillus was studied.
First, the nuclease S1, which is absolutely specific to the single-stranded segments of the nucleic acids, was isolated and purified to homogeneous condition.
For the first time the laboratory isolated new purine nucleoside phosphorylase (PNP) II from E.coli K-12 and PNP from the kidney, spleen, and embryos of rabbit,
also from the healthy and tumour tissues of human lung and kidney that were homogenized until homogen condition via affinity chromatography and their physical-chemical
and catalytic properties were being studied. The screening of a number several tens of purine nucleosides derivatives was carried out to obtain strong specific enzyme
inhibitors for creating immunodeficient conditions, if necessary. Several compounds of acyclic guanosine derivatives were discovered that effectively inhibit the
enzyme from tumor tissue. Proved to be that PNP, and BB and MM isoenzymes of CK are biomarkers of organo-toxic action of 1.3 diazaadamantan with antitumor activity. Great work has been done for the study of the impact of environmentally adverse factors on enzyme systems. In particular, the activity levels of CK, PNP, and aspartate
and alanine aminotransferases (AST, ALT) were defined in the blood serum of the workers from the chloroprene workshop of the "Nairit" factory and from the foil
workshop of the "Kanaz'' factory, also the influence of ukrinol on the vitality of some organs (liver, brain, heart) was studied on experimental animals. The next important step of the laboratory's work became the elaboration of a new drug "Immunomodulator" that is high-efficient immunostimulant non-specific drug
based on Ca-modified double-stranded RNA, which is intended for the prophylaxy of a number of viral diseases of farm animals. The drug is hallmarked in the Ministry
of Agriculture. The permission for its production has been received. The drug is patented and has a copyright certificate and certificates of the Ministry of Agriculture.
Current research projects:
«Technology Pilot production of the antiviral drug, immunomodulator.»
Currently, work is underway to study the effect of the mechanisms of ionizing and non-ionizing radiation on the activity of some enzymes (CK, PNP, ALT, AST, ALP). New natural protectors are being searched.
Selected Publications:
>> Full publications list of IMBPatents received: