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Труды сотрудников ИБФ СО РАН

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Investigation of application of PHA coating to enhance biocompatibility of vascular stents / A. V. Protopopov [et al.] // Doklady Biological Sciences. - 2005. - Vol. 401, Is. 1-6. - P85-87, DOI 10.1007/s10630-005-0051-8 . - ISSN 0012-4966
Кл.слова (ненормированные):
biomaterial -- polymer -- animal -- article -- blood vessel transplantation -- chemistry -- dog -- stent -- Animals -- Blood Vessel Prosthesis Implantation -- Coated Materials, Biocompatible -- Dogs -- Polymers -- Stents

Scopus
Держатели документа:
Krasnoyarsk Regional Clinical Hospital No. 1, Krasnoyarsk, Russian Federation
Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation
Krasnoyarsk Regional Postmortem Examination Center, Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Protopopov, A.V.; Kochkina, T.A.; Konstantinov, E.P.; Shishatskaya, E.I.; Efremov, S.N.; Volova, T.G.; Gitelson, I.I.

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Dynamics of amino acid composition of the medium during culture of isolated liver and kidneys by the controlled perfusion method / V. A. Barashkov [et al.] // Bulletin of Experimental Biology and Medicine. - 1976. - Vol. 80, Is. 11. - P1305-1307 . - ISSN 0007-4888
Кл.слова (ненормированные):
amino acid -- dog -- in vitro study -- kidney perfusion -- liver perfusion -- theoretical study
Аннотация: The dynamics of the amino acid composition of the medium was investigated during perfusion of the dog liver and kidney for 6 h with a mixture of autogenous plasma and medium No.199 in the ratio of 2:3. During culture of the kidney for 6 h the histidine concentration in the medium increased by 2.2 times compared with initially, the concentration of glutamic acid by 1.7 times, and of alanine and lysine by 1.6 times, whereas the concentrations of arginine, serine, and aspartic acid fell by 3.3 times and those of glutamine with threonine by 2.5 times. During perfusion of the liver the concentration of glutamic acid rose by 2.9 times, of alanine by 2.3 times, cystine by 2.0 times, and glycine by 1.5 times. The concentration of tyrosine fell by half, and that of phenylalanine and serine by 1.4 times. The arginine concentration fell so quickly during perfusion of the liver that by the second hour after the beginning of perfusion no arginine could be found in the medium. The method of amino acid analysis during organ culture as described can be used as a method of developing and correcting culture media.

Scopus
Держатели документа:
Siberian Div., Dept. Biophys., L.V. Kirenskii Inst. Phys., Acad. Sci. USSR, Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Barashkov, V.A.; Gitel'zon, I.I.; Nefedov, V.P.; Trubachev, I.N.

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Dynamics of amino acid composition of the medium in isolated organ culture by the controlled perfusion method / V. A. Barashkov [et al.] // Bulletin of Experimental Biology and Medicine. - 1975. - Vol. 80, Is. 7. - P759-761 . - ISSN 0007-4888
Кл.слова (ненормированные):
amino acid -- tissue culture medium -- dog -- in vitro study -- organ culture -- organ perfusion -- theoretical study
Аннотация: The dynamics of the amino acid composition of the perfusion fluid was investigated during adequate perfusion of isolated dog organs (the thorax and a complex consisting of the thoracic organs, kidneys, and liver). The concentration of amino acids such as histidine, lysine, and alanine in the perfusion fluid 6 h after the beginning of perfusion of the organ complex was higher, whereas that of arginine, serine, aspartic acid, threonine with glutamine, isoleucine, proline, leucine, and valine was much lower than initially. In experiments on the isolated thorax the dynamics of the amino acid composition of the medium was studied during perfusion for 4 h. The concentration of alanine, lysine, and histidine in the medium increased, whereas those of serine, aspartic acid, isoleucine, tyrosine, and phenylalanine decreased.

Scopus
Держатели документа:
Siberian Div., Dept. Biophys., L.V. Kirenskii Inst. Phys., Acad. Sci. USSR, Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Barashkov, V.A.; Gitel'zon, I.I.; Nefedov, V.P.; Trubachev, I.N.

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Effect of hypoxemia on erythropoietic activity of perfused organs / I. I. Gitelzon, V. P. Nefedov, V. V. Mezhevikin // Byulleten Eksperimentalnoi Biologii i Meditsiny. - 1977. - Vol. 84, Is. 7. - С. 23-24 . - ISSN 0365-9615
Кл.слова (ненормированные):
animal -- bone marrow -- cell proliferation -- erythropoiesis -- histology -- hypoxemia -- injury -- mammal -- perfusion fluid -- theoretical study -- article -- dog -- kidney -- liver -- metabolism -- perfusion -- spleen -- sternum -- erythropoietin -- Animal -- Anoxemia -- Dogs -- English Abstract -- Erythropoietin -- Kidney -- Liver -- Perfusion -- Spleen -- Sternum

Scopus
Держатели документа:
L.V. Kirensky Inst. Phys., Siberian Branch USSR Acad. Sci., Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Gitelzon, I.I.; Nefedov, V.P.; Mezhevikin, V.V.

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The dynamics of the amino acid composition of the medium in cultivating the isolated organs by controlled perfusion (Russian) / V. A. Barashkov [и др.] // Byulleten Eksperimentalnoi Biologii i Meditsiny. - 1975. - Vol. 80, Is. 7. - С. 36-38 . - ISSN 0365-9615
Кл.слова (ненормированные):
amino acid -- amino acid -- dog -- in vitro study -- kidney -- liver -- sternum -- theoretical study -- animal -- article -- culture medium -- metabolism -- organ culture -- organ preservation -- perfusion -- tissue preservation -- kidney -- liver -- kidney perfusion -- liver perfusion -- tissue culture -- Amino Acids -- Animal -- Culture Media -- Dogs -- English Abstract -- In Vitro -- Organ Culture -- Organ Preservation -- Perfusion -- Tissue Preservation -- Kidney -- Liver

Scopus
Держатели документа:
L.V. Kirensky Inst. Phys., Siberian Branch, USSR Acad. Sci., Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Barashkov, V.A.; Gitelzon, I.I.; Nefedov, V.P.; Trubachev, I.N.

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Study of the immunogenicity of the VP2 protein of canine parvovirus produced using an improved Baculovirus expression system / D. Chang, Y. Liu, Y. Chen [et al.] // BMC Vet. Res. - 2020. - Vol. 16, Is. 1. - Ст. 202, DOI 10.1186/s12917-020-02422-3 . - ISSN 1746-6148
Кл.слова (ненормированные):
Baculovirus expression system -- Canine parvovirus -- VP2 protein -- canine parvovirus vaccine -- protein VP2 -- recombinant protein -- unclassified drug -- virus antibody -- virus vaccine -- affinity chromatography -- animal experiment -- antibody titer -- Article -- baculovirus expression system -- Canine parvovirus -- controlled study -- DNA transposition -- enzyme linked immunosorbent assay -- female -- fluorescence microscopy -- gene expression level -- hemagglutination inhibition -- hemagglutination inhibition test -- immunogenicity -- mouse -- nonhuman -- parvovirus infection -- protein expression -- Sf9 cell line -- vaccination -- Western blotting
Аннотация: Background: Canine parvovirus (CPV) is now recognized as a serious threat to the dog breeding industry worldwide. Currently used CPV vaccines all have their specific drawbacks, prompting a search for alternative safe and effective vaccination strategies such as subunit vaccine. VP2 protein is the major antigen targeted for developing CPV subunit vaccine, however, its production in baculovirus expression system remains challenging due to the insufficient yield. Therefore, our study aims to increase the VP2 protein production by using an improved baculovirus expression system and to evaluate the immunogenicity of the purified VP2 protein in mice. Results: The results showed that high-level expression of the full length VP2 protein was achieved using our modified baculovirus expression system. The recombinant virus carrying two copies of VP2 gene showed the highest expression level, with a productivity of 186 mg/L, which is about 1.4-1.6 fold that of the recombinant viruses carrying only one copy. The purified protein reacted with Mouse anti-His tag monoclonal antibody and Rabbit anti-VP2 polyclonal antibody. BALB/c mice were intramuscularly immunized with purified VP2 protein twice at 2 week intervals. After vaccination, VP2 protein could induce the mice produce high level of hemagglutination inhibition antibodies. Conclusions: Full length CPV VP2 protein was expressed at high level and purified efficiently. Moreover, it stimulated mice to produce high level of antibodies with hemmaglutination inhibition properties. The VP2 protein expressed in this study could be used as a putative economic and efficient subunit vaccine against CPV infection. © 2020 The Author(s).

Scopus
Держатели документа:
Henan Provincal Engineering and Technology Center of Health Products for Livestock and Poultry, Key Laboratory of Ecological Security, Collab. Innov. Ctr. of Water Secty. for Water Src. Reg. of Mid-line of S.-to-N. Diversion Proj. of Henan Prov., School of Agricultural Engineering, Nanyang Normal University, Nanyang, 473061, China
Institute of Biophysics, Siberian Branch, Russian Academy of Science, Federal Research Center Krasnoyarsk Science Center SB RAS, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Chang, D.; Liu, Y.; Chen, Y.; Hu, X.; Burov, A.; Puzyr, A.; Bondar, V.; Yao, L.

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Study of the immunogenicity of the VP2 protein of canine parvovirus produced using an improved Baculovirus expression system / D. Chang, Y. K. Liu, Y. Y. Chen [et al.] // BMC Vet. Res. - 2020. - Vol. 16, Is. 1. - Ст. 202, DOI 10.1186/s12917-020-02422-3. - Cited References:30. - This work was financially supported by the National Natural Science Foundation of China (No. 31870917), The program for Innovative Research Team of Science and Technology in University of Henan Province (No. 20IRTSTHN024) and Key Scientific Research Projects of Colleges and Universities in Henan Province of China (No. 18B230008). The funding bodies played no role in the design of the study, the collection, analysis, and interpretation of data and in writing the manuscript. . - ISSN 1746-6148

РУБ Veterinary Sciences
Рубрики:
VIRUS-LIKE PARTICLES
   ESCHERICHIA-COLI
   GENETIC-ANALYSIS
   CPV-VP2
Кл.слова (ненормированные):
Canine parvovirus -- VP2 protein -- Baculovirus expression system
Аннотация: Background Canine parvovirus (CPV) is now recognized as a serious threat to the dog breeding industry worldwide. Currently used CPV vaccines all have their specific drawbacks, prompting a search for alternative safe and effective vaccination strategies such as subunit vaccine. VP2 protein is the major antigen targeted for developing CPV subunit vaccine, however, its production in baculovirus expression system remains challenging due to the insufficient yield. Therefore, our study aims to increase the VP2 protein production by using an improved baculovirus expression system and to evaluate the immunogenicity of the purified VP2 protein in mice. Results The results showed that high-level expression of the full length VP2 protein was achieved using our modified baculovirus expression system. The recombinant virus carrying two copies of VP2 gene showed the highest expression level, with a productivity of 186 mg/L, which is about 1.4-1.6 fold that of the recombinant viruses carrying only one copy. The purified protein reacted with Mouse anti-His tag monoclonal antibody and Rabbit anti-VP2 polyclonal antibody. BALB/c mice were intramuscularly immunized with purified VP2 protein twice at 2 week intervals. After vaccination, VP2 protein could induce the mice produce high level of hemagglutination inhibition antibodies. Conclusions Full length CPV VP2 protein was expressed at high level and purified efficiently. Moreover, it stimulated mice to produce high level of antibodies with hemmaglutination inhibition properties. The VP2 protein expressed in this study could be used as a putative economic and efficient subunit vaccine against CPV infection.

WOS
Держатели документа:
Nanyang Normal Univ, Sch Agr Engn, Henan Provincal Engn & Technol Ctr Hlth Prod Live, Nanyang 473061, Peoples R China.
Nanyang Normal Univ, Sch Agr Engn, Key Lab Ecol Secur, Nanyang 473061, Peoples R China.
Nanyang Normal Univ, Sch Agr Engn, Collaborat Innovat Ctr Water Secur Water Source R, Nanyang 473061, Peoples R China.
Russian Acad Sci, Fed Res Ctr, Krasnoyarsk Sci Ctr, Inst Biophys,Siberian Branch, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Chang, Dao; Liu, Yangkun; Chen, Yangyang; Hu, Xiaomin; Burov, Andrey; Puzyr, Alexey; Bondar, Vladimir; Yao, Lunguang; National Natural Science Foundation of ChinaNational Natural Science Foundation of China [31870917]; program for Innovative Research Team of Science and Technology in University of Henan Province [20IRTSTHN024]; Key Scientific Research Projects of Colleges and Universities in Henan Province of China [18B230008]

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